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1fw8
From Proteopedia
(New page: 200px<br /><applet load="1fw8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fw8, resolution 2.3Å" /> '''CIRCULARLY PERMUTED P...) |
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| - | [[Image:1fw8.gif|left|200px]]<br /><applet load="1fw8" size=" | + | [[Image:1fw8.gif|left|200px]]<br /><applet load="1fw8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fw8, resolution 2.3Å" /> | caption="1fw8, resolution 2.3Å" /> | ||
'''CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72'''<br /> | '''CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 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 | + | 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 Structure== | ==About this Structure== | ||
| - | 1FW8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ACE and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1FW8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two-domain protein]] | [[Category: two-domain protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:16 2008'' |
Revision as of 10:43, 21 February 2008
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CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72
Overview
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 Structure
1FW8 is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Phosphoglycerate kinase, with EC number 2.7.2.3 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:43:16 2008
Categories: Phosphoglycerate kinase | Saccharomyces cerevisiae | Single protein | Bizebard, T. | Desmadril, M. | Minard, P. | Ritco-Vonsovici, M. | Tougard, P. | ACE | GOL | Glycolysis | Kinase | Mutant | Permutation | Permuted sequence | Pgk | Phosphotransferase | Protein folding | Two-domain protein
