4cge

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(Difference between revisions)

Revision as of 18:58, 5 August 2016

Crystal structure of Mycobacterium tuberculosis Resuscitation promoting factor E

Structural highlights

4cge is a 6 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RPFE_MYCTU] Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity.^[1] Stimulates growth of stationary phase M.bovis (a slow-growing Mycobacterium), reduces the lag phase of diluted fast-growers M.smegmatis and Micrococcus luteus. Sequential gene disruption indicates RpfB and RpfE are higher than RpfD and RpfC in functional hierarchy.^[2]

Publication Abstract from PubMed

Resuscitation promoting factor (Rpf) proteins, which hydrolyze the sugar chains in cell-wall peptidoglycan (PG), play key roles in prokaryotic cell elongation, division and escape from dormancy to vegetative growth. Like other bacteria, Mycobacterium tuberculosis (Mtb) expresses multiple Rpfs, none of which is individually essential. This redundancy has left unclear the distinct functions of the different Rpfs. To explore the distinguishing characteristics of the five Mtb Rpfs, we determined the crystal structure of the RpfE catalytic domain. The protein adopts the characteristic Rpf fold, but the catalytic cleft is narrower compared to Mtb RpfB. Also in contrast to RpfB, in which the substrate-binding surfaces are negatively charged, the corresponding RpfE catalytic pocket and predicted peptide-binding sites are more positively charged at neutral pH. The complete reversal of the electrostatic potential of the substrate-binding site suggests that the different Rpfs function optimally at different pHs or most efficiently hydrolyze different micro-domains of PG. These studies provide insights into the molecular determinants of the evolution of functional specialization in Rpfs.

Mycobacterium tuberculosis RpfE crystal structure reveals a positively charged catalytic cleft.,Mavrici D, Prigozhin DM, Alber T Protein Sci. 2014 Jan 22. doi: 10.1002/pro.2431. PMID:24452911^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mukamolova GV, Turapov OA, Young DI, Kaprelyants AS, Kell DB, Young M. A family of autocrine growth factors in Mycobacterium tuberculosis. Mol Microbiol. 2002 Nov;46(3):623-35. PMID:12410821
↑ Mukamolova GV, Turapov OA, Young DI, Kaprelyants AS, Kell DB, Young M. A family of autocrine growth factors in Mycobacterium tuberculosis. Mol Microbiol. 2002 Nov;46(3):623-35. PMID:12410821
↑ Mavrici D, Prigozhin DM, Alber T. Mycobacterium tuberculosis RpfE crystal structure reveals a positively charged catalytic cleft. Protein Sci. 2014 Jan 22. doi: 10.1002/pro.2431. PMID:24452911 doi:http://dx.doi.org/10.1002/pro.2431

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cge"

Categories: Alber, T | Mavrici, D | Prigozhin, D M | Hydrolase | Secreted protein

@@ Line 1: / Line 1: @@
 ==Crystal structure of Mycobacterium tuberculosis Resuscitation promoting factor E==
 <StructureSection load='4cge' size='340' side='right' caption='[[4cge]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4cge]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CGE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CGE FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cge OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cge RCSB], [http://www.ebi.ac.uk/pdbsum/4cge PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cge OCA], [http://pdbe.org/4cge PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cge RCSB], [http://www.ebi.ac.uk/pdbsum/4cge PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cge ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4cge" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4cge

From Proteopedia

Revision as of 18:58, 5 August 2016

Crystal structure of Mycobacterium tuberculosis Resuscitation promoting factor E

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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