4lvq
From Proteopedia
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| - | + | ==Crystal structure of the M. tuberculosis phosphate binding protein PstS3== | |
| - | + | <StructureSection load='4lvq' size='340' side='right' caption='[[4lvq]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4lvq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVQ FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pstS3, phoS2, Rv0928, MT0955, MTCY21C12.22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lvq RCSB], [http://www.ebi.ac.uk/pdbsum/4lvq PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mycobacterium tuberculosis evades host immune responses by colonizing macrophages. Intraphagosomal M. tuberculosis is exposed to environmental stresses such as reactive oxygen and nitrogen intermediates as well as acid shock and inorganic phosphate (Pi) depletion. Experimental evidence suggests that expression levels of mycobacterial protein PstS3 (Rv0928) are significantly increased when M. tuberculosis bacilli are exposed to Pi starvation. Hence, PstS3 may be important for survival of Mtb in conditions where there is limited supply of Pi. We report here the structure of PstS3 from M. tuberculosis at 2.3-A resolution. The protein presents a structure typical for ABC phosphate transfer receptors. Comparison with its cognate receptor PstS1 showed a different pattern distribution of surface charges in proximity to the Pi recognition site, suggesting complementary roles of the two proteins in Pi uptake. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. | ||
| - | + | Crystal structure of the Mycobacterium tuberculosis phosphate binding protein PstS3.,Ferraris DM, Spallek R, Oehlmann W, Singh M, Rizzi M Proteins. 2014 Mar 11. doi: 10.1002/prot.24548. PMID:24615888<ref>PMID:24615888</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Phosphate-binding protein|Phosphate-binding protein]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ferraris, D M.]] | [[Category: Ferraris, D M.]] | ||
[[Category: Rizzi, M.]] | [[Category: Rizzi, M.]] | ||
Revision as of 03:13, 4 September 2014
Crystal structure of the M. tuberculosis phosphate binding protein PstS3
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