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| | ==Crystal Structure of Phosphoglycerate Kinase from Bacillus Anthracis== | | ==Crystal Structure of Phosphoglycerate Kinase from Bacillus Anthracis== |
| - | <StructureSection load='3uwd' size='340' side='right' caption='[[3uwd]], [[Resolution|resolution]] 1.68Å' scene=''> | + | <StructureSection load='3uwd' size='340' side='right'caption='[[3uwd]], [[Resolution|resolution]] 1.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3uwd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3b2b 3b2b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UWD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3uwd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3b2b 3b2b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UWD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></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]] 1.68Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAS4988, BA_5367, GBAA_5367, pgk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 "Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</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=3uwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uwd OCA], [https://pdbe.org/3uwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uwd RCSB], [https://www.ebi.ac.uk/pdbsum/3uwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uwd ProSAT]</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=3uwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uwd OCA], [http://pdbe.org/3uwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uwd RCSB], [http://www.ebi.ac.uk/pdbsum/3uwd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uwd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PGK_BACAN PGK_BACAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Phosphoglycerate Kinase|Phosphoglycerate Kinase]] | + | *[[Phosphoglycerate kinase 3D structures|Phosphoglycerate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Phosphoglycerate kinase]] | + | [[Category: Bacillus anthracis]] |
| - | [[Category: Anderson, W F]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Anderson WF]] |
| - | [[Category: Chruszcz, M]] | + | [[Category: Chruszcz M]] |
| - | [[Category: Grimshaw, S]] | + | [[Category: Grimshaw S]] |
| - | [[Category: Kudritska, M]] | + | [[Category: Kudritska M]] |
| - | [[Category: Minor, W]] | + | [[Category: Minor W]] |
| - | [[Category: Porebski, P]] | + | [[Category: Porebski P]] |
| - | [[Category: Savchenko, A]] | + | [[Category: Savchenko A]] |
| - | [[Category: Zheng, H]] | + | [[Category: Zheng H]] |
| - | [[Category: Anthrax]]
| + | |
| - | [[Category: Csgid]]
| + | |
| - | [[Category: Phosphoglycerate]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
3uwd is a 1 chain structure with sequence from Bacillus anthracis. This structure supersedes the now removed PDB entry 3b2b. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.68Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PGK_BACAN
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
- ↑ 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
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