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3uqc

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<StructureSection load='3uqc' size='340' side='right'caption='[[3uqc]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
<StructureSection load='3uqc' size='340' side='right'caption='[[3uqc]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3uqc]] is a 4 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=3UQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UQC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3uqc]] is a 4 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=3UQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UQC 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=SIN:SUCCINIC+ACID'>SIN</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]] 2.256&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3otv|3otv]], [[3ouk|3ouk]], [[3oun|3oun]]</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=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT4029, Rv3910 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=3uqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uqc OCA], [https://pdbe.org/3uqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uqc RCSB], [https://www.ebi.ac.uk/pdbsum/3uqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uqc 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=3uqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uqc OCA], [http://pdbe.org/3uqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uqc RCSB], [http://www.ebi.ac.uk/pdbsum/3uqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uqc ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MVIN_MYCTO MVIN_MYCTO]] Essential for cell growth and peptidoglycan synthesis.
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[https://www.uniprot.org/uniprot/MVINL_MYCTU MVINL_MYCTU] Essential for cell growth and peptidoglycan synthesis.<ref>PMID:22275220</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Prokaryotic cell wall biosynthesis is coordinated with cell growth and division, but the mechanisms regulating this dynamic process remain obscure. Here, we describe a phosphorylation-dependent regulatory complex that controls peptidoglycan (PG) biosynthesis in Mycobacterium tuberculosis. We found that PknB, a PG-responsive Ser-Thr protein kinase (STPK), initiates complex assembly by phosphorylating a kinase-like domain in the essential PG biosynthetic protein, MviN. This domain was structurally diverged from active kinases and did not mediate phosphotransfer. Threonine phosphorylation of the pseudokinase domain recruited the FhaA protein through its forkhead-associated (FHA) domain. The crystal structure of this phosphorylated pseudokinase-FHA domain complex revealed the basis of FHA domain recognition, which included unexpected contacts distal to the phosphorylated threonine. Conditional degradation of these proteins in mycobacteria demonstrated that MviN was essential for growth and PG biosynthesis and that FhaA regulated these processes at the cell poles and septum. Controlling this spatially localized PG regulatory complex is only one of several cellular roles ascribed to PknB, suggesting that the capacity to coordinate signaling across multiple processes is an important feature conserved between eukaryotic and prokaryotic STPK networks.
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A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria.,Gee CL, Papavinasasundaram KG, Blair SR, Baer CE, Falick AM, King DS, Griffin JE, Venghatakrishnan H, Zukauskas A, Wei JR, Dhiman RK, Crick DC, Rubin EJ, Sassetti CM, Alber T Sci Signal. 2012 Jan 24;5(208):ra7. PMID:22275220<ref>PMID:22275220</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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<div class="pdbe-citations 3uqc" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alber, T]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Blair, S R]]
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[[Category: Alber T]]
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[[Category: Gee, C L]]
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[[Category: Blair SR]]
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[[Category: Structural genomic]]
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[[Category: Gee CL]]
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[[Category: Fhaa]]
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[[Category: Kinase fold]]
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[[Category: Tbsgc]]
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[[Category: Transferase]]
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Current revision

Structure of the Intracellular Kinase Homology Domain of Rv3910 at 2.2 A resolution

PDB ID 3uqc

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