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6drq

From Proteopedia

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m (Protected "6drq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6drq is ON HOLD until Paper Publication
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==The crystal structure of SatS c-terminal domain in complex with bromine==
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<StructureSection load='6drq' size='340' side='right'caption='[[6drq]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6drq]] is a 1 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=6DRQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DRQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LH57_18085 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=6drq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6drq OCA], [http://pdbe.org/6drq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6drq RCSB], [http://www.ebi.ac.uk/pdbsum/6drq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6drq ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The SecA2 protein export system is critical for the virulence of Mycobacterium tuberculosis. However, the mechanism of this export pathway remains unclear. Through a screen for suppressors of a secA2 mutant, we identified a new player in the mycobacterial SecA2 pathway that we named SatS for SecA2 (two) Suppressor. In M. tuberculosis, SatS is required for the export of a subset of SecA2 substrates and for growth in macrophages. We further identify a role for SatS as a protein export chaperone. SatS exhibits multiple properties of a chaperone, including the ability to bind to and protect substrates from aggregation. Our structural studies of SatS reveal a distinct combination of a new fold and hydrophobic grooves resembling preprotein-binding sites of the SecB chaperone. These results are significant in better defining a molecular pathway for M. tuberculosis pathogenesis and in expanding our appreciation of the diversity among chaperones and protein export systems.
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Authors: Hughes, R.C., Sacchettini, J.C., TB Structural Genomics Consortium (TBSGC)
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Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway.,Miller BK, Hughes R, Ligon LS, Rigel NW, Malik S, Anjuwon-Foster BR, Sacchettini JC, Braunstein M Elife. 2019 Jan 3;8. pii: 40063. doi: 10.7554/eLife.40063. PMID:30604681<ref>PMID:30604681</ref>
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Description: The crystal structure of SatS c-terminal domain in complex with bromine
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Hughes, R.C]]
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<div class="pdbe-citations 6drq" style="background-color:#fffaf0;"></div>
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[[Category: Sacchettini, J.C]]
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== References ==
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[[Category: Tb Structural Genomics Consortium (Tbsgc)]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Myctu]]
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[[Category: Hughes, R C]]
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[[Category: Sacchettini, J C]]
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[[Category: Structural genomic]]
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[[Category: Chaperone]]
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[[Category: Protein export]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Seca2]]
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[[Category: Tbsgc]]

Revision as of 10:14, 18 December 2019

The crystal structure of SatS c-terminal domain in complex with bromine

PDB ID 6drq

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