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1jdw

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(New page: 200px<br /> <applet load="1jdw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdw, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE A...)
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[[Image:1jdw.gif|left|200px]]<br />
 
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<applet load="1jdw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jdw, resolution 1.90&Aring;" />
 
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'''CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS==
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L-arginine:glycine amidinotransferase (AT) catalyses the committed step in, creatine biosynthesis by formation of guanidinoacetic acid, the immediate, precursor of creatine. We have determined the crystal structure of the, recombinant human enzyme by multiple isomorphous replacement at 1.9 A, resolution. A telluromethionine derivative was used in sequence, assignment. The structure of AT reveals a new fold with 5-fold, pseudosymmetry of circularly arranged betabeta alphabeta-modules. These, enclose the active site compartment, which is accessible only through a, narrow channel. The overall structure resembles a basket with handles that, are formed from insertions into the betabeta alphabeta-modules. Binding of, L-ornithine, a product inhibitor, reveals a marked induced-fit mechanism, with a loop at the active site entrance changing its conformation, accompanied by a shift of an alpha-helix by -4 A. Binding of the arginine, educt to the inactive mutant C407A shows a similar mode of binding. A, reaction mechanism with a catalytic triad Cys-His-Asp is proposed on the, basis of substrate and product bound states.
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<StructureSection load='1jdw' size='340' side='right'caption='[[1jdw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1jdw]] is a 1 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=1JDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDW FirstGlance]. <br>
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Known diseases associated with this structure: AGAT deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602360 602360]]
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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]] 1.9&#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=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
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==About this Structure==
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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=1jdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdw OCA], [https://pdbe.org/1jdw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jdw RCSB], [https://www.ebi.ac.uk/pdbsum/1jdw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdw ProSAT]</span></td></tr>
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1JDW 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 BME as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycine_amidinotransferase Glycine amidinotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.4.1 2.1.4.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JDW OCA].
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</table>
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== Disease ==
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==Reference==
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[https://www.uniprot.org/uniprot/GATM_HUMAN GATM_HUMAN] Defects in GATM are the cause of arginine:glycine amidinotransferase deficiency (AGAT deficiency) [MIM:[https://omim.org/entry/612718 612718]. AGAT deficiency is an autosomal recessive disorder characterized by developmental delay/regression, mental retardation, severe disturbance of expressive and cognitive speech, and severe depletion of creatine/phosphocreatine in the brain.
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Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis., Humm A, Fritsche E, Steinbacher S, Huber R, EMBO J. 1997 Jun 16;16(12):3373-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9218780 9218780]
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== Function ==
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[[Category: Glycine amidinotransferase]]
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[https://www.uniprot.org/uniprot/GATM_HUMAN GATM_HUMAN] Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development. May be involved in the response to heart failure by elevating local creatine synthesis.<ref>PMID:16820567</ref> <ref>PMID:16125225</ref> <ref>PMID:16614068</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/jd/1jdw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1jdw ConSurf].
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<div style="clear:both"></div>
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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: Fritsche, E.]]
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[[Category: Fritsche E]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Humm, A.]]
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[[Category: Humm A]]
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[[Category: Steinbacher, S.]]
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[[Category: Steinbacher S]]
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[[Category: BME]]
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[[Category: catalytic triad]]
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[[Category: creatine biosynthesis]]
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[[Category: fivefold pseudosymmetry]]
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[[Category: novel fold]]
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[[Category: reaction mechanism]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:39:53 2007''
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Current revision

CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS

PDB ID 1jdw

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