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| {{STRUCTURE_1fw8| PDB=1fw8 | SCENE= }} | | {{STRUCTURE_1fw8| PDB=1fw8 | SCENE= }} |
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| '''CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72'''
| | ===CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12454459}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12454459 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12454459}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Phosphotransferase]] | | [[Category: Phosphotransferase]] |
| [[Category: Protein folding,two-domain protein]] | | [[Category: Protein folding,two-domain protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:50:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:02:17 2008'' |