3q3v: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 3: Line 3:
<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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3Q3V FirstGlance]. <br>
<table><tr><td colspan='2'>[[3q3v]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3Q3V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.145&#8491;</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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cj1402c, pgk ([https://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'>[https://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3q3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q3v OCA], [https://pdbe.org/3q3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q3v RCSB], [https://www.ebi.ac.uk/pdbsum/3q3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q3v ProSAT]</span></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=3q3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q3v OCA], [https://pdbe.org/3q3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q3v RCSB], [https://www.ebi.ac.uk/pdbsum/3q3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q3v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PGK_CAMJE PGK_CAMJE]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 26: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Camje]]
[[Category: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phosphoglycerate kinase]]
[[Category: Anderson WF]]
[[Category: Anderson, W F]]
[[Category: Edwards A]]
[[Category: Structural genomic]]
[[Category: Filippova EV]]
[[Category: Edwards, A]]
[[Category: Onopriyenko O]]
[[Category: Filippova, E V]]
[[Category: Savchenko A]]
[[Category: Onopriyenko, O]]
[[Category: Wawrzak Z]]
[[Category: Savchenko, A]]
[[Category: Wawrzak, Z]]
[[Category: Converts 3-phospho-d-glycerate to 3-phospho-d-glyceroyl phosphate during the glycolysis pathway]]
[[Category: Csgid]]
[[Category: Pgk]]
[[Category: Transferase]]

Latest revision as of 13:20, 6 November 2024

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 Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.145Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PGK_CAMJE

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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA