Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Pubmed ID :18682225
Publication Date : //

The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation.


RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli. Here, we present the crystal structure of the E. coli RNase E catalytic domain in the apo-state at 3.3 A. This structure indicates that, upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site. The structural data suggest a mechanism of RNA recognition and cleavage that explains the enzyme's preference for substrates possessing a 5'-monophosphate and accounts for the protective effect of a triphosphate cap for most transcripts. Internal flexibility within the quaternary structure is also observed, a finding that has implications for recognition of structured RNA substrates and for the mechanism of internal entry for a subset of substrates that are cleaved without 5'-end requirements.

Authors : Koslover Daniel J , Callaghan Anastasia J , Marcaida Maria J , Garman Elspeth F , Martick Monika , Scott William G , Luisi Ben F ,

Related products :

Catalog number Product name Quantity
29-378 Of the multiple RNases H in mammals, RNase HI is the major enzyme and shows increased activity during DNA replication. It shows more homology to the RNase HII of Escherichia coli.Of the multiple RNase 0.1 mg
29-377 Of the multiple RNases H in mammals, RNase HI is the major enzyme and shows increased activity during DNA replication. It shows more homology to the RNase HII of Escherichia coli.Of the multiple RNase 0.05 mg
P92387Hu01 Charcot Leyden Crystal Protein (CLC) Organism: Homo sapiens (Human) Source: Escherichia coli 50ug
P92387Hu01 Charcot Leyden Crystal Protein (CLC) Organism: Homo sapiens (Human) Source: Escherichia coli 10ug
P92387Hu01 Charcot Leyden Crystal Protein (CLC) Organism: Homo sapiens (Human) Source: Escherichia coli 100ug
29-820 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.1 mg
29-822 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.1 mg
29-819 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.1 mg
25-857 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.05 mg
29-821 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.1 mg
29-845 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.1 mg
25-815 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.05 mg
25-818 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.05 mg
29-823 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.1 mg
29-862 The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes 0.1 mg
29-767 The function remains unknown.The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at l 0.1 mg
29-824 UBE2L3 (ubiquitin-conjugating enzyme E2L 3) Antibody The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiq 0.05 mg
orb41518 UBE2G2 antibody Polyclonal Rabbit polyclonal to UBE2G2. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. U 100
orb41534 UBE4B antibody Polyclonal Rabbit polyclonal to UBE4B. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubi 100
orb40792 UBE2B antibody Polyclonal Rabbit polyclonal to UBE2B. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubi 100
orb41092 Ube2L3 antibody Polyclonal Rabbit polyclonal to Ube2L3. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. U 100
H-2782.0025 rec Human Pancreatic Ribonuclease (RNase) (expressed in E.coli) Salt _ Binding _ Synonym rec Ribonuclease (RNase), rec Pancreatic Ribonuclease (RNase) SumFormula 25.0 mg
H-2782.0005 rec Human Pancreatic Ribonuclease (RNase) (expressed in E.coli) Salt _ Binding _ Synonym rec Ribonuclease (RNase), rec Pancreatic Ribonuclease (RNase) SumFormula 5.0 mg
26-565 DCP1B may play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It may remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5' 0.05 mg
15-288-10801F Ribonuclease pancreatic - EC 3.1.27.5; RNase 1; RNase A; RNase UpI-1; RIB-1; HP-RNase Polyclonal 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur