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==Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.==
==Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.==
<StructureSection load='3q3v' size='340' side='right' caption='[[3q3v]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3q3v' size='340' side='right' caption='[[3q3v]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3q3v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_nctc_11168_=_atcc_700819 Campylobacter jejuni subsp. jejuni nctc 11168 = atcc 700819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q3V FirstGlance]. <br>
<table><tr><td colspan='2'>[[3q3v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Camje Camje]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q3V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cj1402c, pgk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192222 Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cj1402c, pgk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192222 CAMJE])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </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=3q3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q3v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q3v RCSB], [http://www.ebi.ac.uk/pdbsum/3q3v 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=3q3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q3v OCA], [http://pdbe.org/3q3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q3v RCSB], [http://www.ebi.ac.uk/pdbsum/3q3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q3v ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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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 3q3v" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Campylobacter jejuni subsp. jejuni nctc 11168 = atcc 700819]]
[[Category: Camje]]
[[Category: Phosphoglycerate kinase]]
[[Category: Phosphoglycerate kinase]]
[[Category: Anderson, W F]]
[[Category: Anderson, W F]]

Revision as of 15:35, 11 August 2016

Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.

Structural highlights

3q3v is a 2 chain structure with sequence from Camje. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:
Gene:Cj1402c, pgk (CAMJE)
Activity:Phosphoglycerate kinase, with EC number 2.7.2.3
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Phosphoglycerate kinase (PGK) is indispensable during glycolysis for anaerobic glucose degradation and energy generation. Here we present comprehensive structure analysis of two putative PGKs from Bacillus anthracis str. Sterne and Campylobacter jejuni in the context of their structural homologs. They are the first PGKs from pathogenic bacteria reported in the Protein Data Bank. The crystal structure of PGK from Bacillus anthracis str. Sterne (BaPGK) has been determined at 1.68 A while the structure of PGK from Campylobacter jejuni (CjPGK) has been determined at 2.14 A resolution. The proteins' monomers are composed of two domains, each containing a Rossmann fold, hinged together by a helix which can be used to adjust the relative position between two domains. It is also shown that apo-forms of both BaPGK and CjPGK adopt open conformations as compared to the substrate and ATP bound forms of PGK from other species.

Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni.,Zheng H, Filippova EV, Tkaczuk KL, Dworzynski P, Chruszcz M, Porebski PJ, Wawrzak Z, Onopriyenko O, Kudritska M, Grimshaw S, Savchenko A, Anderson WF, Minor W J Struct Funct Genomics. 2012 Mar;13(1):15-26. Epub 2012 Mar 10. PMID:22403005[1]

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

See Also

References

  1. Zheng H, Filippova EV, Tkaczuk KL, Dworzynski P, Chruszcz M, Porebski PJ, Wawrzak Z, Onopriyenko O, Kudritska M, Grimshaw S, Savchenko A, Anderson WF, Minor W. Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni. J Struct Funct Genomics. 2012 Mar;13(1):15-26. Epub 2012 Mar 10. PMID:22403005 doi:10.1007/s10969-012-9131-9

3q3v, resolution 2.15Å

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