3q3v: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.== | ||
<StructureSection load='3q3v' size='340' side='right' caption='[[3q3v]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== 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> | |||
</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='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='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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:22403005</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Phosphoglycerate Kinase|Phosphoglycerate Kinase]] | *[[Phosphoglycerate Kinase|Phosphoglycerate Kinase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Campylobacter jejuni subsp. jejuni nctc 11168 = atcc 700819]] | [[Category: Campylobacter jejuni subsp. jejuni nctc 11168 = atcc 700819]] | ||
[[Category: Phosphoglycerate kinase]] | [[Category: Phosphoglycerate kinase]] | ||
[[Category: Anderson, W F | [[Category: Anderson, W F]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Edwards, A | [[Category: Edwards, A]] | ||
[[Category: Filippova, E V | [[Category: Filippova, E V]] | ||
[[Category: Onopriyenko, O | [[Category: Onopriyenko, O]] | ||
[[Category: Savchenko, A | [[Category: Savchenko, A]] | ||
[[Category: Wawrzak, Z | [[Category: Wawrzak, Z]] | ||
[[Category: Converts 3-phospho-d-glycerate to 3-phospho-d-glyceroyl phosphate during the glycolysis pathway]] | [[Category: Converts 3-phospho-d-glycerate to 3-phospho-d-glyceroyl phosphate during the glycolysis pathway]] | ||
[[Category: Csgid]] | [[Category: Csgid]] | ||
[[Category: Pgk]] | [[Category: Pgk]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 13:07, 20 January 2015
Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.
Structural highlights
Publication Abstract from PubMedPhosphoglycerate 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 AlsoReferences
|
| ||||||||||||||||||||||