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2geu

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Revision as of 07:52, 18 October 2017

Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-II (RT)

Structural highlights

2geu is a 1 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2ges, 2get, 2gev
Gene:	coaA(Rv1092c) (MYCTU)
Activity:	Pantothenate kinase, with EC number 2.7.1.33
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Pantothenate kinase (PanK) is a ubiquitous and essential enzyme that catalyzes the first step of the universal coenzyme A biosynthetic pathway. In this step, pantothenate (vitamin B(5)) is converted to 4'-phosphopantothenate, which subsequently forms coenzyme A in four enzymatic steps. The complex of this enzyme from Mycobacterium tuberculosis (MtPanK) with a derivative of the feedback inhibitor coenzyme A has been crystallized in two forms and its structure solved. The structure was refined in both forms using room-temperature and low-temperature X-ray data. In both forms, the MtPanK subunit has a mononucleotide-binding fold with a seven-stranded central beta-sheet and helices on either side. However, there is a small though significant difference in subunit association between the two forms. The structure is also grossly similar to the enzyme from Escherichia coli. The active-site pocket and the dimeric interface are on two opposite sides of the PanK subunit. The enzymes from M. tuberculosis and E. coli exhibit several differences, particularly at the dimeric interface. On the other hand, the coenzyme A-binding region is almost entirely conserved. A delineation of the invariant and variable features of the PanK structure further indicates that the dimeric interface is very variable, while the coenzyme A-binding site is substantially invariant. A sequence alignment involving various bacterial PanKs is in agreement with this conclusion. The strong correlation between structural plasticity, evolutionary conservation and variability and function exhibited by the molecule could be important in the design of species-specific inhibitors of the enzyme.

Invariance and variability in bacterial PanK: a study based on the crystal structure of Mycobacterium tuberculosis PanK.,Das S, Kumar P, Bhor V, Surolia A, Vijayan M Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):628-38. Epub 2006, May 12. PMID:16699190^[1]

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

References

↑ Das S, Kumar P, Bhor V, Surolia A, Vijayan M. Invariance and variability in bacterial PanK: a study based on the crystal structure of Mycobacterium tuberculosis PanK. Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):628-38. Epub 2006, May 12. PMID:16699190 doi:10.1107/S0907444906012728

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2geu"

@@ Line 1: / Line 1: @@
 ==Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-II (RT)==
 <StructureSection load='2geu' size='340' side='right' caption='[[2geu]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
@@ Line 8: / Line 9: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">coaA(Rv1092c) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantothenate_kinase Pantothenate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.33 2.7.1.33] </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=2geu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2geu OCA], [http://pdbe.org/2geu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2geu RCSB], [http://www.ebi.ac.uk/pdbsum/2geu 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=2geu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2geu OCA], [http://pdbe.org/2geu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2geu RCSB], [http://www.ebi.ac.uk/pdbsum/2geu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2geu ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 2geu" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Pantothenate kinase|Pantothenate kinase]]
 == References ==
 <references/>

2geu

From Proteopedia

Revision as of 07:52, 18 October 2017

Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-II (RT)

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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