1ush
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known | + | The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system. |
==About this Structure== | ==About this Structure== | ||
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[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
| - | [[Category: 5'-nucleotidase]] | ||
[[Category: hydrolase (phosphoric monoester)]] | [[Category: hydrolase (phosphoric monoester)]] | ||
[[Category: periplasmic protein]] | [[Category: periplasmic protein]] | ||
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[[Category: udp-sugar hydrolase]] | [[Category: udp-sugar hydrolase]] | ||
| - | ''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 15:27:48 2008'' |
Revision as of 13:27, 21 February 2008
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5'-NUCLEOTIDASE FROM E. COLI
Overview
The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system.
About this Structure
1USH is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as 5'-nucleotidase, with EC number 3.1.3.5 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site., Knofel T, Strater N, Nat Struct Biol. 1999 May;6(5):448-53. PMID:10331872
Page seeded by OCA on Thu Feb 21 15:27:48 2008
