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==CRYSTAL FORM I OF THE D93N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS==
==CRYSTAL FORM I OF THE D93N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS==
<StructureSection load='4anc' size='340' side='right' caption='[[4anc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='4anc' size='340' side='right'caption='[[4anc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4anc]] 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=4ANC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ANC FirstGlance]. <br>
<table><tr><td colspan='2'>[[4anc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ANC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ANC FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k44|1k44]], [[4and|4and]], [[4ane|4ane]]</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]] 2.8&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=4anc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4anc OCA], [https://pdbe.org/4anc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4anc RCSB], [https://www.ebi.ac.uk/pdbsum/4anc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4anc 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=4anc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4anc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4anc RCSB], [http://www.ebi.ac.uk/pdbsum/4anc PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NDK_MYCTU NDK_MYCTU]] Major role in the synthesis of nucleoside triphosphates other than ATP.[HAMAP-Rule:MF_00451]  
[https://www.uniprot.org/uniprot/NDK_MYCTU NDK_MYCTU] Major role in the synthesis of nucleoside triphosphates other than ATP.[HAMAP-Rule:MF_00451]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4anc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Nucleoside diphosphate kinase|Nucleoside diphosphate kinase]]
*[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Nucleoside-diphosphate kinase]]
[[Category: Dautant A]]
[[Category: Dautant, A]]
[[Category: Georgescauld F]]
[[Category: Georgescauld, F]]
[[Category: Habersetzer J]]
[[Category: Habersetzer, J]]
[[Category: Lascu I]]
[[Category: Lascu, I]]
[[Category: Moynie L]]
[[Category: Moynie, L]]
[[Category: Transferase]]

Latest revision as of 14:30, 20 December 2023

CRYSTAL FORM I OF THE D93N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSISCRYSTAL FORM I OF THE D93N MUTANT OF NUCLEOSIDE DIPHOSPHATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS

Structural highlights

4anc is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NDK_MYCTU Major role in the synthesis of nucleoside triphosphates other than ATP.[HAMAP-Rule:MF_00451]

Publication Abstract from PubMed

Most nucleoside diphosphate kinases (NDPKs) are hexamers. The C-terminal tail interacting with the neighboring subunits is crucial for hexamer stability. In the NDPK from Mycobacterium tuberculosis (Mt) this tail is missing. The quaternary structure of Mt-NDPK is essential for full enzymatic activity and for protein stability to thermal and chemical denaturation. We identified the intersubunit salt bridge Arg(80)-Asp(93) as essential for hexamer stability, compensating for the decreased intersubunit contact area. Breaking the salt bridge by the mutation D93N dramatically decreased protein thermal stability. The mutation also decreased stability to denaturation by urea and guanidinium. The D93N mutant was still hexameric and retained full activity. When exposed to low concentrations of urea it dissociated into folded monomers followed by unfolding while dissociation and unfolding of the wild type simultaneously occur at higher urea concentrations. The dissociation step was not observed in guanidine hydrochloride, suggesting that low concentration of salt may stabilize the hexamer. Indeed, guanidinium and many other salts stabilized the hexamer with a half maximum effect of about 0.1 M, increasing protein thermostability. The crystal structure of the D93N mutant has been solved.

Intersubunit Ionic Interactions Stabilize the Nucleoside Diphosphate Kinase of Mycobacterium tuberculosis.,Georgescauld F, Moynie L, Habersetzer J, Cervoni L, Mocan I, Borza T, Harris P, Dautant A, Lascu I PLoS One. 2013;8(3):e57867. doi: 10.1371/journal.pone.0057867. Epub 2013 Mar 5. PMID:23526954[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Georgescauld F, Moynie L, Habersetzer J, Cervoni L, Mocan I, Borza T, Harris P, Dautant A, Lascu I. Intersubunit Ionic Interactions Stabilize the Nucleoside Diphosphate Kinase of Mycobacterium tuberculosis. PLoS One. 2013;8(3):e57867. doi: 10.1371/journal.pone.0057867. Epub 2013 Mar 5. PMID:23526954 doi:http://dx.doi.org/10.1371/journal.pone.0057867

4anc, resolution 2.80Å

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