1hjk: Difference between revisions
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==Overview== | ==Overview== | ||
Using a mutant version of E. coli alkaline phosphatase, we succeeded in | Using a mutant version of E. coli alkaline phosphatase, we succeeded in trapping and determining the structure of the phospho-enzyme intermediate. The X-ray structure also revealed the catalytic water molecule, bound to one of the active site zinc ions, positioned ideally for the apical attack necessary for the hydrolysis of the intermediate. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kantrowitz, E | [[Category: Kantrowitz, E R.]] | ||
[[Category: Ma, L.]] | [[Category: Ma, L.]] | ||
[[Category: Murphy, J | [[Category: Murphy, J E.]] | ||
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: transferase(phospho]] | [[Category: transferase(phospho]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:54 2008'' | ||
Revision as of 11:01, 21 February 2008
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ALKALINE PHOSPHATASE MUTANT H331Q
Overview
Using a mutant version of E. coli alkaline phosphatase, we succeeded in trapping and determining the structure of the phospho-enzyme intermediate. The X-ray structure also revealed the catalytic water molecule, bound to one of the active site zinc ions, positioned ideally for the apical attack necessary for the hydrolysis of the intermediate.
About this Structure
1HJK is a Single protein structure of sequence from Escherichia coli with ZN, MG and SO4 as ligands. Active as Alkaline phosphatase, with EC number 3.1.3.1 Known structural/functional Sites: CTA and CTB. Full crystallographic information is available from OCA.
Reference
Trapping and visualization of a covalent enzyme-phosphate intermediate., Murphy JE, Stec B, Ma L, Kantrowitz ER, Nat Struct Biol. 1997 Aug;4(8):618-22. PMID:9253408
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