4cmx

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{{STRUCTURE_4cmx| PDB=4cmx | SCENE= }}
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==Crystal structure of Rv3378c==
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===Crystal structure of Rv3378c===
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<StructureSection load='4cmx' size='340' side='right' caption='[[4cmx]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
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{{ABSTRACT_PUBMED_24516143}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4cmx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CMX FirstGlance]. <br>
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==Function==
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BHC:BENZENE+HEXACARBOXYLIC+ACID'>BHC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cmv|4cmv]], [[4cmw|4cmw]]</td></tr>
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<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=4cmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cmx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cmx RCSB], [http://www.ebi.ac.uk/pdbsum/4cmx PDBsum]</span></td></tr>
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</table>
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== Function ==
[[http://www.uniprot.org/uniprot/TUBOL_MYCTU TUBOL_MYCTU]] Catalyzes the PP-removal from tuberculosinyl diphosphate to produce both tubercilosinol and isotuberculosinol. Can also use labdadienyl diphosphates, copalyl diphosphate (CDP), ent-CDP and syn-CDP in vitro.
[[http://www.uniprot.org/uniprot/TUBOL_MYCTU TUBOL_MYCTU]] Catalyzes the PP-removal from tuberculosinyl diphosphate to produce both tubercilosinol and isotuberculosinol. Can also use labdadienyl diphosphates, copalyl diphosphate (CDP), ent-CDP and syn-CDP in vitro.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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To identify lipids with roles in tuberculosis disease, we systematically compared the lipid content of virulent Mycobacterium tuberculosis with the attenuated vaccine strain Mycobacterium bovis bacillus Calmette-Guerin. Comparative lipidomics analysis identified more than 1,000 molecular differences, including a previously unknown, Mycobacterium tuberculosis-specific lipid that is composed of a diterpene unit linked to adenosine. We established the complete structure of the natural product as 1-tuberculosinyladenosine (1-TbAd) using mass spectrometry and NMR spectroscopy. A screen for 1-TbAd mutants, complementation studies, and gene transfer identified Rv3378c as necessary for 1-TbAd biosynthesis. Whereas Rv3378c was previously thought to function as a phosphatase, these studies establish its role as a tuberculosinyl transferase and suggest a revised biosynthetic pathway for the sequential action of Rv3377c-Rv3378c. In agreement with this model, recombinant Rv3378c protein produced 1-TbAd, and its crystal structure revealed a cis-prenyl transferase fold with hydrophobic residues for isoprenoid binding and a second binding pocket suitable for the nucleoside substrate. The dual-substrate pocket distinguishes Rv3378c from classical cis-prenyl transferases, providing a unique model for the prenylation of diverse metabolites. Terpene nucleosides are rare in nature, and 1-TbAd is known only in Mycobacterium tuberculosis. Thus, this intersection of nucleoside and terpene pathways likely arose late in the evolution of the Mycobacterium tuberculosis complex; 1-TbAd serves as an abundant chemical marker of Mycobacterium tuberculosis, and the extracellular export of this amphipathic molecule likely accounts for the known virulence-promoting effects of the Rv3378c enzyme.
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==About this Structure==
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Molecular profiling of Mycobacterium tuberculosis identifies tuberculosinyl nucleoside products of the virulence-associated enzyme Rv3378c.,Layre E, Lee HJ, Young DC, Jezek Martinot A, Buter J, Minnaard AJ, Annand JW, Fortune SM, Snider BB, Matsunaga I, Rubin EJ, Alber T, Moody DB Proc Natl Acad Sci U S A. 2014 Feb 10. PMID:24516143<ref>PMID:24516143</ref>
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[[4cmx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024516143</ref><references group="xtra"/><references/>
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</div>
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[[Category: Alber, T.]]
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== References ==
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[[Category: Annand, J W.]]
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<references/>
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[[Category: Buter, J.]]
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__TOC__
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[[Category: Fortune, S M.]]
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</StructureSection>
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[[Category: Layre, E.]]
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[[Category: Myctu]]
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[[Category: Lee, H J.]]
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[[Category: Alber, T]]
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[[Category: Martinot, A J.]]
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[[Category: Annand, J W]]
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[[Category: Matsunaga, I.]]
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[[Category: Buter, J]]
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[[Category: Minnaard, A J.]]
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[[Category: Fortune, S M]]
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[[Category: Moody, D B.]]
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[[Category: Layre, E]]
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[[Category: Rubin, E J.]]
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[[Category: Lee, H J]]
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[[Category: Snider, B B.]]
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[[Category: Martinot, A J]]
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[[Category: Young, D C.]]
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[[Category: Matsunaga, I]]
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[[Category: Minnaard, A J]]
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[[Category: Moody, D B]]
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[[Category: Rubin, E J]]
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[[Category: Snider, B B]]
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[[Category: Young, D C]]
[[Category: Nuclear protein]]
[[Category: Nuclear protein]]

Revision as of 18:39, 24 December 2014

Crystal structure of Rv3378c

4cmx, resolution 2.36Å

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