1a7a
From Proteopedia
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|PDB= 1a7a |SIZE=350|CAPTION= <scene name='initialview01'>1a7a</scene>, resolution 2.8Å | |PDB= 1a7a |SIZE=350|CAPTION= <scene name='initialview01'>1a7a</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ADC:(1'R,2'S)-9-(2-HYDROXY-3'-KETO-CYCLOPENTEN-1-YL)ADENINE'>ADC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7a OCA], [http://www.ebi.ac.uk/pdbsum/1a7a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a7a RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
S-Adenosylhomocysteine (AdoHcy) hydrolase regulates all adenosylmethionine-(AdoMet) dependent transmethylations by hydrolyzing the potent feedback inhibitor AdoHcy to homocysteine and adenosine. The crystallographic structure determination of a selenomethionyl-incorporated AdoHcy hydrolase inhibitor complex was accomplished using single wavelength anomalous diffraction data and the direct methods program, Snb v2.0, which produced the positions of all 30 crystallographically distinct selenium atoms. The mode of enzyme-cofactor binding is unique, requiring interactions from two protein monomers. An unusual dual role for a catalytic water molecule in the active site is revealed in the complex with the adenosine analog 2'-hydroxy, 3'-ketocyclopent-4'-enyladenine. | S-Adenosylhomocysteine (AdoHcy) hydrolase regulates all adenosylmethionine-(AdoMet) dependent transmethylations by hydrolyzing the potent feedback inhibitor AdoHcy to homocysteine and adenosine. The crystallographic structure determination of a selenomethionyl-incorporated AdoHcy hydrolase inhibitor complex was accomplished using single wavelength anomalous diffraction data and the direct methods program, Snb v2.0, which produced the positions of all 30 crystallographically distinct selenium atoms. The mode of enzyme-cofactor binding is unique, requiring interactions from two protein monomers. An unusual dual role for a catalytic water molecule in the active site is revealed in the complex with the adenosine analog 2'-hydroxy, 3'-ketocyclopent-4'-enyladenine. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Hypermethioninemia with deficiency of S-adenosylhomocysteine hydrolase OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=180960 180960]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Turner, M A.]] | [[Category: Turner, M A.]] | ||
[[Category: Yuan, C S.]] | [[Category: Yuan, C S.]] | ||
| - | [[Category: ADC]] | ||
| - | [[Category: NAD]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: nad binding protein]] | [[Category: nad binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:48 2008'' |
Revision as of 15:34, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Adenosylhomocysteinase, with EC number 3.3.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH
Overview
S-Adenosylhomocysteine (AdoHcy) hydrolase regulates all adenosylmethionine-(AdoMet) dependent transmethylations by hydrolyzing the potent feedback inhibitor AdoHcy to homocysteine and adenosine. The crystallographic structure determination of a selenomethionyl-incorporated AdoHcy hydrolase inhibitor complex was accomplished using single wavelength anomalous diffraction data and the direct methods program, Snb v2.0, which produced the positions of all 30 crystallographically distinct selenium atoms. The mode of enzyme-cofactor binding is unique, requiring interactions from two protein monomers. An unusual dual role for a catalytic water molecule in the active site is revealed in the complex with the adenosine analog 2'-hydroxy, 3'-ketocyclopent-4'-enyladenine.
About this Structure
1A7A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength., Turner MA, Yuan CS, Borchardt RT, Hershfield MS, Smith GD, Howell PL, Nat Struct Biol. 1998 May;5(5):369-76. PMID:9586999
Page seeded by OCA on Sun Mar 30 18:34:48 2008
