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2obm

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Revision as of 08:56, 18 October 2017

Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria

Structural highlights

2obm is a 1 chain structure with sequence from Eco27. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2obl
Gene:	escN (ECO27)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The type III secretion system (T3SS) ATPase is the conserved and essential inner-membrane component involved in the initial stages of selective secretion of specialized T3SS virulence effector proteins from the bacterial cytoplasm through to the infected host cell, a process crucial to subsequent pathogenicity. Here we present the 1.8-A-resolution crystal structure of the catalytic domain of the prototypical T3SS ATPase EscN from enteropathogenic Escherichia coli (EPEC). Along with in vitro and in vivo mutational analysis, our data show that the T3SS ATPases share similarity with the F1 ATPases but have important structural and sequence differences that dictate their unique secretory role. We also show that T3SS ATPase activity is dependent on EscN oligomerization and describe the molecular features and possible functional implications of a hexameric ring model.

Structural analysis of a prototypical ATPase from the type III secretion system.,Zarivach R, Vuckovic M, Deng W, Finlay BB, Strynadka NC Nat Struct Mol Biol. 2007 Feb;14(2):131-7. Epub 2007 Jan 21. PMID:17237797^[1]

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

References

↑ Zarivach R, Vuckovic M, Deng W, Finlay BB, Strynadka NC. Structural analysis of a prototypical ATPase from the type III secretion system. Nat Struct Mol Biol. 2007 Feb;14(2):131-7. Epub 2007 Jan 21. PMID:17237797 doi:10.1038/nsmb1196

1 Structural highlights
2 Evolutionary Conservation
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/2obm"

@@ Line 1: / Line 1: @@
 ==Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria==
 <StructureSection load='2obm' size='340' side='right' caption='[[2obm]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2obl|2obl]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">escN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=574521 ECO27])</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=2obm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obm OCA], [http://pdbe.org/2obm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2obm RCSB], [http://www.ebi.ac.uk/pdbsum/2obm PDBsum]</span></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=2obm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obm OCA], [http://pdbe.org/2obm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2obm RCSB], [http://www.ebi.ac.uk/pdbsum/2obm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2obm ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

2obm

From Proteopedia

Revision as of 08:56, 18 October 2017

Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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