4ane: Difference between revisions
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==R80N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS== | ==R80N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS== | ||
<StructureSection load='4ane' size='340' side='right' caption='[[4ane]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4ane' size='340' side='right' caption='[[4ane]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k44|1k44]], [[4anc|4anc]], [[4and|4and]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k44|1k44]], [[4anc|4anc]], [[4and|4and]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </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=4ane FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ane OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ane RCSB], [http://www.ebi.ac.uk/pdbsum/4ane PDBsum]</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=4ane FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ane OCA], [http://pdbe.org/4ane PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ane RCSB], [http://www.ebi.ac.uk/pdbsum/4ane PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ane ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ane" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 13:32, 5 August 2016
R80N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSISR80N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS
Structural highlights
Function[NDK_MYCTU] Major role in the synthesis of nucleoside triphosphates other than ATP.[HAMAP-Rule:MF_00451] Publication Abstract from PubMedThe crystal structure of the wild-type nucleoside diphosphate kinase from Mycobacterium tuberculosis at 2.6 A resolution revealed that the intersubunit salt bridge Arg80-Asp93 contributes to the thermal stability of the hexamer (Tm = 76 degrees C). On mutating Asp93 to Asn to break the salt bridge, the thermal stability dramatically decreased by 27.6 degrees C. Here, on mutating Arg80 to Asn, the thermal stability also significantly decreased by 8.0 degrees C. In the X-ray structure of the R80N mutant solved at 1.9 A resolution the salt bridge was replaced by intersubunit hydrogen bonds that contribute to the thermal stability of the hexamer. A citrate anion from the crystallization buffer was bound at the bottom of the nucleotide-binding site via electrostatic and hydrogen-bonding interactions with six conserved residues involved in nucleotide binding. Structural analysis shows that the citrate is present at the location of the nucleotide phosphate groups. Structure of Mycobacterium tuberculosis nucleoside diphosphate kinase R80N mutant in complex with citrate.,Georgescauld F, Moynie L, Habersetzer J, Dautant A Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):40-3. doi:, 10.1107/S2053230X13034134. Epub 2013 Dec 24. PMID:24419614[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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