3ne0
From Proteopedia
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==Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation== | ==Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation== | ||
| - | <StructureSection load='3ne0' size='340' side='right' caption='[[3ne0]], [[Resolution|resolution]] 1.00Å' scene=''> | + | <StructureSection load='3ne0' size='340' side='right'caption='[[3ne0]], [[Resolution|resolution]] 1.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3ne0]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3ne0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NE0 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1Å</td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ne0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne0 OCA], [https://pdbe.org/3ne0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ne0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ne0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne0 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/RIPA_MYCTU RIPA_MYCTU] Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages.<ref>PMID:16495549</ref> <ref>PMID:17919286</ref> <ref>PMID:18463693</ref> <ref>PMID:20826344</ref> <ref>PMID:21864539</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ne0 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ne0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cell separation depends on cell-wall hydrolases that cleave the peptidoglycan layer connecting daughter cells. In Mycobacterium tuberculosis, this process is governed by the predicted endopeptidase RipA. In the absence of this enzyme, the bacterium is unable to divide and exhibits an abnormal phenotype. We here report the crystal structure of a relevant portion of RipA, containing its catalytic-domain and an extra-domain of hitherto unknown function. The structure clearly demonstrates that RipA is produced as a zymogen, which needs to be activated to achieve cell-division. Bacterial cell-wall degradation assays and proteolysis experiments strongly suggest that activation occurs via proteolytic processing of a fully solvent exposed loop identified in the crystal structure. Indeed, proteolytic cleavage at this loop produces an activated form, consisting of the sole catalytic domain. Our work provides the first evidence of self-inhibition in cell-disconnecting enzymes and opens a field for the design of novel antitubercular therapeutics. | ||
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| - | Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation.,Ruggiero A, Marasco D, Squeglia F, Soldini S, Pedone E, Pedone C, Berisio R Structure. 2010 Sep 8;18(9):1184-90. PMID:20826344<ref>PMID:20826344</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3ne0" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: | + | [[Category: Berisio R]] |
| - | [[Category: | + | [[Category: Ruggiero A]] |
| - | [[Category: | + | [[Category: Squeglia F]] |
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Current revision
Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation
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