3nwy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:31, 21 February 2024) (edit) (undo)
 
Line 1: Line 1:
==Structure and allosteric regulation of the uridine monophosphate kinase from Mycobacterium tuberculosis==
==Structure and allosteric regulation of the uridine monophosphate kinase from Mycobacterium tuberculosis==
-
<StructureSection load='3nwy' size='340' side='right' caption='[[3nwy]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
+
<StructureSection load='3nwy' size='340' side='right'caption='[[3nwy]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3nwy]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NWY FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3nwy]] is a 6 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=3NWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NWY FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 2.54&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT2951, MTCY274.14c, pyrH, Rv2883c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UMP_kinase UMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.22 2.7.4.22] </span></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=3nwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nwy OCA], [https://pdbe.org/3nwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nwy RCSB], [https://www.ebi.ac.uk/pdbsum/3nwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nwy 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=3nwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nwy OCA], [http://pdbe.org/3nwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nwy RCSB], [http://www.ebi.ac.uk/pdbsum/3nwy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nwy ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/PYRH_MYCTU PYRH_MYCTU]] Catalyzes the reversible phosphorylation of UMP to UDP.[HAMAP-Rule:MF_01220]
+
[https://www.uniprot.org/uniprot/PYRH_MYCTU PYRH_MYCTU] Catalyzes the reversible phosphorylation of UMP to UDP.[HAMAP-Rule:MF_01220]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 21: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3nwy ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3nwy ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
Nucleoside Monophosphate Kinases (NMPKs) family are key enzymes in nucleotide metabolism. Bacterial UMPKs depart from the main superfamily of NMPKs. Having no eukaryotic counterparts they represent attractive therapeutic targets. They are regulated by GTP and UTP, while showing different mechanisms in Gram(+), Gram(-) and archaeal bacteria. In this work, we have characterized the mycobacterial UMPK (UMPKmt) combining enzymatic and structural investigations with site-directed mutagenesis. UMPKmt exhibits cooperativity toward ATP and an allosteric regulation by GTP and UTP. The crystal structure of the complex of UMPKmt with GTP solved at 2.5 A, was merely identical to the modelled apo-form, in agreement with SAXS experiments. Only a small stretch of residues was affected upon nucleotide binding, pointing out the role of macromolecular dynamics rather than major structural changes in the allosteric regulation of bacterial UMPKs. We further probe allosteric regulation by site-directed mutagenesis. In particular, a key residue involved in the allosteric regulation of this enzyme was identified.
 
- 
-
Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation.,Labesse G, Benkali K, Salard-Arnaud I, Gilles AM, Munier-Lehmann H Nucleic Acids Res. 2011 Apr 1;39(8):3458-72. Epub 2010 Dec 10. PMID:21149268<ref>PMID:21149268</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 3nwy" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Uridylate kinase|Uridylate kinase]]
*[[Uridylate kinase|Uridylate kinase]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Myctu]]
+
[[Category: Large Structures]]
-
[[Category: UMP kinase]]
+
[[Category: Mycobacterium tuberculosis H37Rv]]
-
[[Category: Labesse, G]]
+
[[Category: Labesse G]]
-
[[Category: Munier-Lehmann, H]]
+
[[Category: Munier-Lehmann H]]
-
[[Category: Aak fold]]
+
-
[[Category: Allosterically activated form]]
+
-
[[Category: Transferase]]
+
-
[[Category: Ump kinase]]
+

Current revision

Structure and allosteric regulation of the uridine monophosphate kinase from Mycobacterium tuberculosis

PDB ID 3nwy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools