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| | ==Crystal Structure of Resuscitation Promoting Factor C== | | ==Crystal Structure of Resuscitation Promoting Factor C== |
| - | <StructureSection load='4ow1' size='340' side='right' caption='[[4ow1]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4ow1' size='340' side='right'caption='[[4ow1]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ow1]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OW1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OW1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ow1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OW1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=4ow1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ow1 OCA], [http://pdbe.org/4ow1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ow1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ow1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ow1 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=4ow1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ow1 OCA], [https://pdbe.org/4ow1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ow1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ow1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ow1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RPFC_MYCTU RPFC_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.<ref>PMID:12410821</ref> 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.<ref>PMID:12410821</ref> | + | [https://www.uniprot.org/uniprot/RPFC_MYCTU RPFC_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.<ref>PMID:12410821</ref> 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.<ref>PMID:12410821</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chauviac, F X]] | + | [[Category: Large Structures]] |
| - | [[Category: Cohen-Gonsaud, M]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Keep, N H]] | + | [[Category: Chauviac FX]] |
| - | [[Category: Quay, D H.X]] | + | [[Category: Cohen-Gonsaud M]] |
| - | [[Category: Peptidoglycan]] | + | [[Category: Keep NH]] |
| - | [[Category: Resuscitation promoting factor]] | + | [[Category: Quay DHX]] |
| - | [[Category: Transglycosylase]]
| + | |
| Structural highlights
Function
RPFC_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
The first structure of the catalytic domain of RpfC (Rv1884), one of the resuscitation-promoting factors (RPFs) from Mycobacterium tuberculosis, is reported. The structure was solved using molecular replacement once the space group had been correctly identified as twinned P21 rather than the apparent C2221 by searching for anomalous scattering sites in P1. The structure displays a very high degree of structural conservation with the previously published structures of the catalytic domains of RpfB (Rv1009) and RpfE (Rv2450). This structural conservation highlights the importance of the versatile domain composition of the RPF family.
The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain.,Chauviac FX, Robertson G, Quay DH, Bagneris C, Dumas C, Henderson B, Ward J, Keep NH, Cohen-Gonsaud M Acta Crystallogr F Struct Biol Commun. 2014 Aug 1;70(Pt 8):1022-6. doi:, 10.1107/S2053230X1401317X. Epub 2014 Jul 23. PMID:25084374[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
- ↑ Chauviac FX, Robertson G, Quay DH, Bagneris C, Dumas C, Henderson B, Ward J, Keep NH, Cohen-Gonsaud M. The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain. Acta Crystallogr F Struct Biol Commun. 2014 Aug 1;70(Pt 8):1022-6. doi:, 10.1107/S2053230X1401317X. Epub 2014 Jul 23. PMID:25084374 doi:http://dx.doi.org/10.1107/S2053230X1401317X
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