3gzh

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[[Image:3gzh.png|left|200px]]
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==Crystal structure of phosphate-bound adenylosuccinate lyase from E. coli==
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<StructureSection load='3gzh' size='340' side='right' caption='[[3gzh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3gzh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GZH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECs1603, purB, Z1860 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylosuccinate_lyase Adenylosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.2 4.3.2.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gzh RCSB], [http://www.ebi.ac.uk/pdbsum/3gzh PDBsum]</span></td></tr>
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</table>
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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/gz/3gzh_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/chain_selection.php?pdb_ID=2ata 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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Adenylosuccinate lyase (ASL) is an enzyme from the purine-biosynthetic pathway that catalyzes the cleavage of 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) to 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) and fumarate. ASL is also responsible for the conversion of succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP) and fumarate. Here, the crystal structure of adenylosuccinate lyase from Escherichia coli was determined to 1.9 A resolution. The enzyme adopts a substrate-bound conformation as a result of the presence of two phosphate ions bound in the active site. Comparison with previously solved structures of the apoenzyme and an SAMP-bound H171A mutant reveals a conformational change at His171 associated with substrate binding and confirms the role of this residue as a catalytic acid.
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{{STRUCTURE_3gzh| PDB=3gzh | SCENE= }}
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The structure of phosphate-bound Escherichia coli adenylosuccinate lyase identifies His171 as a catalytic acid.,Kozlov G, Nguyen L, Pearsall J, Gehring K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt, 9):857-61. Epub 2009 Aug 20. PMID:19724117<ref>PMID:19724117</ref>
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===Crystal structure of phosphate-bound adenylosuccinate lyase from E. coli===
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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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{{ABSTRACT_PUBMED_19724117}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[3gzh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GZH OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:019724117</ref><references group="xtra"/>
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[[Category: Adenylosuccinate lyase]]
[[Category: Adenylosuccinate lyase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
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[[Category: Structural genomic]]
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[[Category: Gehring, K.]]
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[[Category: Gehring, K]]
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[[Category: Kozlov, G.]]
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[[Category: Kozlov, G]]
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[[Category: Adenylosuccinate lyase]]
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[[Category: All-helical fold]]
[[Category: All-helical fold]]
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[[Category: Bacterial structural genomics initiative]]
 
[[Category: Bsgi]]
[[Category: Bsgi]]
[[Category: Lyase]]
[[Category: Lyase]]
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[[Category: Montreal-kingston bacterial structural genomics initiative]]
 
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[[Category: Structural genomic]]
 

Revision as of 09:26, 8 December 2014

Crystal structure of phosphate-bound adenylosuccinate lyase from E. coli

3gzh, resolution 1.90Å

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