View source for 3ouk


==Crystal structure of Rv3910 from Mycobacterium Tuberculosis==
<StructureSection load='3ouk' size='340' side='right'caption='[[3ouk]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ouk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OUK FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3otv|3otv]], [[3oun|3oun]], [[3uqc|3uqc]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT4029, Rv3910 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=3ouk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ouk OCA], [https://pdbe.org/3ouk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ouk RCSB], [https://www.ebi.ac.uk/pdbsum/3ouk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ouk ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/MVIN_MYCTO MVIN_MYCTO]] Essential for cell growth and peptidoglycan synthesis. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ouk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Myctu]]
[[Category: Alber, T]]
[[Category: Gee, C L]]
[[Category: Membrane protein]]
[[Category: Peptidoglycan]]
[[Category: Pseudokinase]]
[[Category: Regulation]]
[[Category: Ser/thr kinase]]
[[Category: Transferase]]