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3po8

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Structural and functional analysis of phosphothreonine-dependent FHA domain interactions

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Retrieved from "http://52.214.119.220/wiki/index.php/3po8"

Categories: Large Structures | Mycobacterium tuberculosis | Pennell S | Smerdon SJ

@@ Line 3: / Line 3: @@
 <StructureSection load='3po8' size='340' side='right'caption='[[3po8]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3po8]] is a 1 chain structure with sequence from [https://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=3PO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PO8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3po8]] is a 1 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=3PO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PO8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3poa|3poa]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0020c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=3po8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3po8 OCA], [https://pdbe.org/3po8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3po8 RCSB], [https://www.ebi.ac.uk/pdbsum/3po8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3po8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FHAA_MYCTU FHAA_MYCTU]] Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.<ref>PMID:22275220</ref>
+[https://www.uniprot.org/uniprot/FHAA_MYCTU FHAA_MYCTU] Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.<ref>PMID:22275220</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-FHA domains are well established as phospho-dependent binding modules mediating signal transduction in Ser/Thr kinase signaling networks in both eukaryotic and prokaryotic species. Although they are unique in binding exclusively to phosphothreonine, the basis for this discrimination over phosphoserine has remained elusive. Here, we attempt to dissect overall binding specificity at the molecular level. We first determined the optimal peptide sequence for Rv0020c FHA domain binding by oriented peptide library screening. This served as a basis for systematic mutagenic and binding analyses, allowing us to derive relative thermodynamic contributions of conserved protein and peptide residues to binding and specificity. Structures of phosphopeptide-bound and uncomplexed Rv0020c FHA domain then directed molecular dynamics simulations which show how the extraordinary discrimination in favor of phosphothreonine occurs through formation of additional hydrogen-bonding networks that are ultimately stabilized by van der Waals interactions of the phosphothreonine gamma-methyl group with a conserved pocket on the FHA domain surface.
-Structural and functional analysis of phosphothreonine-dependent FHA domain interactions.,Pennell S, Westcott S, Ortiz-Lombardia M, Patel D, Li J, Nott TJ, Mohammed D, Buxton RS, Yaffe MB, Verma C, Smerdon SJ Structure. 2010 Dec 8;18(12):1587-95. PMID:21134638<ref>PMID:21134638</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3po8" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 25: / Line 15: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Pennell, S]]
+[[Category: Mycobacterium tuberculosis]]
-[[Category: Smerdon, S J]]
+[[Category: Pennell S]]
-[[Category: Fha domain]]
+[[Category: Smerdon SJ]]
-[[Category: Peptide binding protein]]
-[[Category: Synthetic peptide]]

3po8

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Structural and functional analysis of phosphothreonine-dependent FHA domain interactions

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