3po8

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==Structural and functional analysis of phosphothreonine-dependent FHA domain interactions==
==Structural and functional analysis of phosphothreonine-dependent FHA domain interactions==
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<StructureSection load='3po8' size='340' side='right' caption='[[3po8]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='3po8' size='340' side='right'caption='[[3po8]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3po8]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PO8 FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3poa|3poa]]</td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0020c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr>
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<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>
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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=3po8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3po8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3po8 RCSB], [http://www.ebi.ac.uk/pdbsum/3po8 PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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>
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Pennell, S]]
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[[Category: Pennell S]]
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[[Category: Smerdon, S J]]
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[[Category: Smerdon SJ]]
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[[Category: Fha domain]]
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[[Category: Peptide binding protein]]
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[[Category: Synthetic peptide]]
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Current revision

Structural and functional analysis of phosphothreonine-dependent FHA domain interactions

PDB ID 3po8

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