View source for 5xlw


==Mycobacterium tuberculosis Pantothenate kinase mutant F247A/F254A==
<StructureSection load='5xlw' size='340' side='right'caption='[[5xlw]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xlw]] is a 2 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=5XLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XLW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5xlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xlw OCA], [https://pdbe.org/5xlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xlw RCSB], [https://www.ebi.ac.uk/pdbsum/5xlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xlw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COAA_MYCTU COAA_MYCTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase have been prepared and biochemically and structurally characterized. The mutants were designed to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region. In three of the four crystallographically independent mutant molecules the structure is similar to that in the E. coli enzyme. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. This work demonstrates that the structure of the mycobacterial enzyme can be transformed into a structure similar to that of the E. coli enzyme through minor perturbations without external influences such as those involving ligand binding.

Biochemical and structural studies of mutants indicate concerted movement of the dimer interface and ligand-binding region of Mycobacterium tuberculosis pantothenate kinase.,Paul A, Kumar P, Surolia A, Vijayan M Acta Crystallogr F Struct Biol Commun. 2017 Nov 1;73(Pt 11):635-643. doi:, 10.1107/S2053230X17015667. Epub 2017 Oct 30. PMID:29095158<ref>PMID:29095158</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xlw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pantothenate kinase 3D structures|Pantothenate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Kumar P]]
[[Category: Paul A]]
[[Category: Surolia A]]
[[Category: Vijayan M]]