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==Crystal structure of Rv3910 from Mycobacterium Tuberculosis==
==Crystal structure of Rv3910 from Mycobacterium Tuberculosis==
<StructureSection load='3ouk' size='340' side='right' caption='[[3ouk]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='3ouk' size='340' side='right'caption='[[3ouk]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ouk]] 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=3OUK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OUK FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ouk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. 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">[[3otv|3otv]], [[3oun|3oun]], [[3uqc|3uqc]]</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]] 3.402&#8491;</td></tr>
<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 Mycobacterium tuberculosis])</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>
<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=3ouk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ouk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ouk RCSB], [http://www.ebi.ac.uk/pdbsum/3ouk PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/O05435_MYCTU O05435_MYCTU]] Essential for cell growth and peptidoglycan synthesis.  
[https://www.uniprot.org/uniprot/MVINL_MYCTU MVINL_MYCTU] Essential for cell growth and peptidoglycan synthesis.<ref>PMID:22275220</ref>  
<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>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mycobacterium tuberculosis]]
[[Category: Large Structures]]
[[Category: Alber, T]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Gee, C L]]
[[Category: Alber T]]
[[Category: Membrane protein]]
[[Category: Gee CL]]
[[Category: Peptidoglycan]]
[[Category: Pseudokinase]]
[[Category: Regulation]]
[[Category: Ser/thr kinase]]
[[Category: Transferase]]

Latest revision as of 14:18, 21 February 2024

Crystal structure of Rv3910 from Mycobacterium TuberculosisCrystal structure of Rv3910 from Mycobacterium Tuberculosis

Structural highlights

3ouk is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.402Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MVINL_MYCTU Essential for cell growth and peptidoglycan synthesis.[1]

References

  1. ↑ 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. A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria. Sci Signal. 2012 Jan 24;5(208):ra7. PMID:22275220 doi:10.1126/scisignal.2002525

3ouk, resolution 3.40Å

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