1a7a
From Proteopedia
(New page: 200px<br /> <applet load="1a7a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a7a, resolution 2.8Å" /> '''STRUCTURE OF HUMAN P...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1a7a.gif|left|200px]]<br /> | + | [[Image:1a7a.gif|left|200px]]<br /><applet load="1a7a" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a7a" size=" | + | |
caption="1a7a, resolution 2.8Å" /> | caption="1a7a, resolution 2.8Å" /> | ||
'''STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH'''<br /> | '''STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH'''<br /> | ||
==Overview== | ==Overview== | ||
| - | S-Adenosylhomocysteine (AdoHcy) hydrolase regulates all | + | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1A7A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAD and ADC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1A7A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=ADC:'>ADC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7A OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Borchardt, R | + | [[Category: Borchardt, R T.]] |
| - | [[Category: Hershfield, M | + | [[Category: Hershfield, M S.]] |
| - | [[Category: Howell, P | + | [[Category: Howell, P L.]] |
| - | [[Category: Smith, G | + | [[Category: Smith, G D.]] |
| - | [[Category: Turner, M | + | [[Category: Turner, M A.]] |
| - | [[Category: Yuan, C | + | [[Category: Yuan, C S.]] |
[[Category: ADC]] | [[Category: ADC]] | ||
[[Category: NAD]] | [[Category: NAD]] | ||
| Line 29: | Line 28: | ||
[[Category: nad binding protein]] | [[Category: nad binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:39 2008'' |
Revision as of 09:41, 21 February 2008
|
STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH
Contents |
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.
Disease
Known diseases associated with this structure: Hypermethioninemia with deficiency of S-adenosylhomocysteine hydrolase OMIM:[180960]
About this Structure
1A7A is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Adenosylhomocysteinase, with EC number 3.3.1.1 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 Thu Feb 21 11:41:39 2008
