2skc
From Proteopedia
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[[Image:2skc.gif|left|200px]] | [[Image:2skc.gif|left|200px]] | ||
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| - | | | + | {{STRUCTURE_2skc| PDB=2skc | SCENE= }} |
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'''PYRIDOXAL PHOSPHORYLASE B IN COMPLEX WITH FLUOROPHOSPHATE, GLUCOSE AND INOSINE-5'-MONOPHOSPHATE''' | '''PYRIDOXAL PHOSPHORYLASE B IN COMPLEX WITH FLUOROPHOSPHATE, GLUCOSE AND INOSINE-5'-MONOPHOSPHATE''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2SKC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry | + | 2SKC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1skc 1skc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SKC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Tsitsanou, K E.]] | [[Category: Tsitsanou, K E.]] | ||
[[Category: Zographos, S E.]] | [[Category: Zographos, S E.]] | ||
| - | [[Category: | + | [[Category: Allosteric enzyme]] |
| - | [[Category: | + | [[Category: Glycogen metabolism]] |
| - | [[Category: | + | [[Category: Glycogen phosphorylase]] |
| - | [[Category: | + | [[Category: Pyridoxal phosphate]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:19:28 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:19, 4 May 2008
PYRIDOXAL PHOSPHORYLASE B IN COMPLEX WITH FLUOROPHOSPHATE, GLUCOSE AND INOSINE-5'-MONOPHOSPHATE
Overview
It has been established that phosphate analogues can activate glycogen phosphorylase reconstituted with pyridoxal in place of the natural cofactor pyridoxal 5'-phosphate (Change YC. McCalmont T, Graves DJ. 1983. Biochemistry 22:4987-4993). Pyridoxal phosphorylase b has been studied by kinetic, ultracentrifugation, and X-ray crystallographic experiments. In solution, the catalytically active species of pyridoxal phosphorylase b adopts a conformation that is more R-state-like than that of native phosphorylase b, but an inactive dimeric species of the enzyme can be stabilized by activator phosphite in combination with the T-state inhibitor glucose. Co-crystals of pyridoxal phosphorylase b complexed with either phosphite, phosphate, or fluorophosphate, the inhibitor glucose, and the weak activator IMP were grown in space group P4(3)2(1)2, with native-like unit cell dimensions, and the structures of the complexes have been refined to give crystallographic R factors of 18.5-19.2%, for data between 8 and 2.4 A resolution. The anions bind tightly at the catalytic site in a similar but not identical position to that occupied by the cofactor 5'-phosphate group in the native enzyme (phosphorus to phosphorus atoms distance = 1.2 A). The structural results show that the structures of the pyridoxal phosphorylase b-anion-glucose-IMP complexes are overall similar to the glucose complex of native T-state phosphorylase b. Structural comparisons suggest that the bound anions, in the position observed in the crystal, might have a structural role for effective catalysis.
About this Structure
2SKC is a Single protein structure of sequence from Oryctolagus cuniculus. This structure supersedes the now removed PDB entry 1skc. Full crystallographic information is available from OCA.
Reference
Activator anion binding site in pyridoxal phosphorylase b: the binding of phosphite, phosphate, and fluorophosphate in the crystal., Oikonomakos NG, Zographos SE, Tsitsanou KE, Johnson LN, Acharya KR, Protein Sci. 1996 Dec;5(12):2416-28. PMID:8976550 Page seeded by OCA on Sun May 4 17:19:28 2008
