1a7a

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[[Image:1a7a.gif|left|200px]]
 
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{{Structure
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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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|PDB= 1a7a |SIZE=350|CAPTION= <scene name='initialview01'>1a7a</scene>, resolution 2.8&Aring;
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<StructureSection load='1a7a' size='340' side='right'caption='[[1a7a]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=ADC:(1&#39;R,2&#39;S)-9-(2-HYDROXY-3&#39;-KETO-CYCLOPENTEN-1-YL)ADENINE'>ADC</scene>
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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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|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]
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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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|GENE=
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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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}}
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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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'''STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH'''
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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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==Overview==
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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 ==
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.
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==Disease==
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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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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]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1A7A is a [[Single protein]] structure of sequence 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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</div>
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<div class="pdbe-citations 1a7a" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9586999 9586999]
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*[[S-adenosylhomocysteine hydrolase|S-adenosylhomocysteine hydrolase]]
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[[Category: Adenosylhomocysteinase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Borchardt, R T.]]
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[[Category: Borchardt RT]]
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[[Category: Hershfield, M S.]]
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[[Category: Hershfield MS]]
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[[Category: Howell, P L.]]
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[[Category: Howell PL]]
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[[Category: Smith, G D.]]
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[[Category: Smith GD]]
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[[Category: Turner, M A.]]
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[[Category: Turner MA]]
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[[Category: Yuan, C S.]]
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[[Category: Yuan C-S]]
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[[Category: ADC]]
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[[Category: NAD]]
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[[Category: hydrolase]]
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[[Category: nad binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:04:56 2008''
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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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