1a7a

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{{Seed}}
 
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[[Image:1a7a.png|left|200px]]
 
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==STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH==
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The line below this paragraph, containing "STRUCTURE_1a7a", creates the "Structure Box" on the page.
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<StructureSection load='1a7a' size='340' side='right'caption='[[1a7a]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1a7a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7A FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADC:(1R,2S)-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></td></tr>
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{{STRUCTURE_1a7a| PDB=1a7a | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7a OCA], [https://pdbe.org/1a7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7a RCSB], [https://www.ebi.ac.uk/pdbsum/1a7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7a ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN] Defects in AHCY are the cause of hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:[https://omim.org/entry/613752 613752]. A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy.<ref>PMID:15024124</ref> <ref>PMID:16736098</ref> <ref>PMID:19177456</ref> <ref>PMID:20852937</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/SAHH_HUMAN SAHH_HUMAN] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.<ref>PMID:12590576</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/1a7a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7a ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH===
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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<ref>PMID:9586999</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1a7a" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9586999}}, adds the Publication Abstract to the page
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*[[S-adenosylhomocysteine hydrolase|S-adenosylhomocysteine hydrolase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9586999 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9586999}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1A7A is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7A OCA].
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==Reference==
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<ref group="xtra">PMID:9586999</ref><references group="xtra"/>
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[[Category: Adenosylhomocysteinase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Borchardt, R T.]]
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[[Category: Large Structures]]
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[[Category: Hershfield, M S.]]
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[[Category: Borchardt RT]]
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[[Category: Howell, P L.]]
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[[Category: Hershfield MS]]
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[[Category: Smith, G D.]]
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[[Category: Howell PL]]
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[[Category: Turner, M A.]]
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[[Category: Smith GD]]
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[[Category: Yuan, C S.]]
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[[Category: Turner MA]]
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[[Category: Hydrolase]]
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[[Category: Yuan C-S]]
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[[Category: Nad binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:24:52 2009''
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Current revision

STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH

PDB ID 1a7a

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