2get

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(New page: 200px<br /><applet load="2get" size="450" color="white" frame="true" align="right" spinBox="true" caption="2get, resolution 2.35&Aring;" /> '''Pantothenate kinase ...)
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[[Image:2get.gif|left|200px]]<br /><applet load="2get" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2get, resolution 2.35&Aring;" />
 
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'''Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-I (LT)'''<br />
 
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==Overview==
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==Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with a coenzyme A derivative, Form-I (LT)==
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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.
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<StructureSection load='2get' size='340' side='right'caption='[[2get]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2get]] is a 1 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=2GET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GET FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=COK:[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxy-oxolan-2-yl]methyl+[hydroxy-[(3R)-3-hydroxy-4-[[3-[2-(2-hydroxyethyldisulfanyl)ethylamino]-3-oxo-propyl]amino]-2,2-dimethyl-4-oxo-butoxy]phosphoryl]+hydrogen+phosphate'>COK</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2get FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2get OCA], [https://pdbe.org/2get PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2get RCSB], [https://www.ebi.ac.uk/pdbsum/2get PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2get ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/COAA_MYCTU COAA_MYCTU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/2get_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2get ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:16699190</ref>
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2GET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with COK and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GET OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16699190 16699190]
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</div>
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[[Category: Mycobacterium tuberculosis]]
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<div class="pdbe-citations 2get" style="background-color:#fffaf0;"></div>
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[[Category: Pantothenate kinase]]
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[[Category: Single protein]]
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[[Category: Bhor, V.]]
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[[Category: Das, S.]]
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[[Category: Kumar, P.]]
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[[Category: Surolia, A.]]
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[[Category: Vijayan, M.]]
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[[Category: COK]]
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[[Category: GOL]]
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[[Category: coa biosynthesis]]
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[[Category: homodimer]]
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[[Category: nucleotide binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:09:41 2007''
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==See Also==
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*[[Pantothenate kinase 3D structures|Pantothenate kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Bhor V]]
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[[Category: Das S]]
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[[Category: Kumar P]]
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[[Category: Surolia A]]
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[[Category: Vijayan M]]

Current revision

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

PDB ID 2get

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