1t8y

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|PDB= 1t8y |SIZE=350|CAPTION= <scene name='initialview01'>1t8y</scene>, resolution 3.00&Aring;
|PDB= 1t8y |SIZE=350|CAPTION= <scene name='initialview01'>1t8y</scene>, resolution 3.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/AMP_nucleosidase AMP nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.4 3.2.2.4]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/AMP_nucleosidase AMP nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.4 3.2.2.4] </span>
|GENE= AMN, B1982, Z3139, ECS2779 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= AMN, B1982, Z3139, ECS2779 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=[[1t8r|1T8R]], [[1t8s|1T8S]], [[1t8w|1T8W]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t8y OCA], [http://www.ebi.ac.uk/pdbsum/1t8y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t8y RCSB]</span>
}}
}}
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[[Category: Ealick, S E.]]
[[Category: Ealick, S E.]]
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
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[[Category: PO4]]
 
[[Category: alpha-beta fold]]
[[Category: alpha-beta fold]]
[[Category: alpha-beta-alpha sandwich]]
[[Category: alpha-beta-alpha sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:15:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:52:59 2008''

Revision as of 20:53, 30 March 2008


PDB ID 1t8y

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands: ,
Gene: AMN, B1982, Z3139, ECS2779 (Escherichia coli)
Activity: AMP nucleosidase, with EC number 3.2.2.4
Related: 1T8R, 1T8S, 1T8W


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of E.coli AMP Nucleosidase complexed with phosphate


Overview

AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to form adenine and ribose 5-phosphate. The enzyme is found only in prokaryotes, where it plays a role in purine nucleoside salvage and intracellular AMP level regulation. Enzyme activity is stimulated by ATP and suppressed by phosphate. The structure of unliganded AMN was determined at 2.7 A resolution, and structures of the complexes with either formycin 5'-monophosphate or inorganic phosphate were determined at 2.6 A and 3.0 A resolution, respectively. AMN is a biological homohexamer, and each monomer is composed of two domains: a catalytic domain and a putative regulatory domain. The overall topology of the catalytic domain and some features of the substrate binding site resemble those of the nucleoside phosphorylases, demonstrating that AMN is a new member of the family. The structure of the regulatory domain consists of a long helix and a four-stranded sheet and has a novel topology.

About this Structure

1T8Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases., Zhang Y, Cottet SE, Ealick SE, Structure. 2004 Aug;12(8):1383-94. PMID:15296732

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