1fw8: Difference between revisions
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|PDB= 1fw8 |SIZE=350|CAPTION= <scene name='initialview01'>1fw8</scene>, resolution 2.3Å | |PDB= 1fw8 |SIZE=350|CAPTION= <scene name='initialview01'>1fw8</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw8 OCA], [http://www.ebi.ac.uk/pdbsum/1fw8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fw8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Ritco-Vonsovici, M.]] | [[Category: Ritco-Vonsovici, M.]] | ||
[[Category: Tougard, P.]] | [[Category: Tougard, P.]] | ||
[[Category: glycolysis]] | [[Category: glycolysis]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
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[[Category: phosphoglycerate kinase]] | [[Category: phosphoglycerate kinase]] | ||
[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
[[Category: protein folding | [[Category: protein folding,two-domain protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:31:26 2008'' |
Revision as of 20:31, 30 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | , | ||||||
Activity: | Phosphoglycerate kinase, with EC number 2.7.2.3 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72
OverviewOverview
The crystallographic structure of a circularly permuted form of yeast PGK, 72p yPGK, has been determined to a resolution of 2.3 A by molecular replacement. In this engineered protein, the C- and N-terminal residues of the wild-type protein are directly connected by a peptide bond and new N- and C-terminal residues are located within the N-terminal domain. The overall fold of the protein is very similar to that of the wild-type protein, directly demonstrating that the continuity of a folding unit is not relevant to the folding process of the whole protein. Only limited structural changes were observed: these were in the regions associated with the new connection, in a long flexible loop in the permuted domain and in the vicinity of Arg38, a functionally important residue. The relative positions of the two domains suggested that this permuted protein adopts one of the most open/twisted conformations seen amongst PGKs of known structure. The effect of the mutation on the functional properties is more easily accounted for by a restriction of hinge-bending motion than by structural changes in the protein.
About this StructureAbout this Structure
1FW8 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a circularly permuted phosphoglycerate kinase., Tougard P, Bizebard T, Ritco-Vonsovici M, Minard P, Desmadril M, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2018-23. Epub 2002, Nov 23. PMID:12454459
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