1fw8: Difference between revisions

Revision as of 13:43, 21 February 2008

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 with and as ligands. Active as Phosphoglycerate kinase, with EC number 2.7.2.3 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

Page seeded by OCA on Thu Feb 21 12:43:16 2008

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OCA

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-[[Image:1fw8.gif|left|200px]]<br /><applet load="1fw8" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1fw8, resolution 2.3&Aring;" />
 '''CIRCULARLY PERMUTED PHOSPHOGLYCERATE KINASE FROM YEAST: PGK P72'''<br />
 ==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.
+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==
-FW8 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FW8 OCA].
+FW8 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==
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 [[Category: two-domain protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:22:04 2007''
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