2ptr

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[[Image:2ptr.jpg|left|200px]]
 
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==Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171A with bound adenylosuccinate substrate==
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The line below this paragraph, containing "STRUCTURE_2ptr", creates the "Structure Box" on the page.
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<StructureSection load='2ptr' size='340' side='right'caption='[[2ptr]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[2ptr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PTR 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]] 1.85&#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=2SA:2-[9-(3,4-DIHYDROXY-5-PHOSPHONOOXYMETHYL-TETRAHYDRO-FURAN-2-YL)-9H-PURIN-6-YLAMINO]-SUCCINIC+ACID'>2SA</scene></td></tr>
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{{STRUCTURE_2ptr| PDB=2ptr | 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=2ptr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ptr OCA], [https://pdbe.org/2ptr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ptr RCSB], [https://www.ebi.ac.uk/pdbsum/2ptr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ptr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PUR8_ECOLI PUR8_ECOLI]
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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/pt/2ptr_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=2ptr ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171A with bound adenylosuccinate substrate'''
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==See Also==
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*[[Adenylosuccinate lyase 3D structures|Adenylosuccinate lyase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Adenylosuccinate lyase (ADL) catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR) to 5-aminoimidazole-4-carboxamide ribotide (AICAR) and fumarate, and of adenylosuccinate (ADS) to adenosine monophosphate (AMP) and fumarate in the de novo purine biosynthetic pathway. ADL belongs to the argininosuccinate lyase (ASL)/fumarase C superfamily of enzymes. Members of this family share several common features including: a mainly alpha-helical, homotetrameric structure; three regions of highly conserved amino acid residues; and a general acid-base catalytic mechanism with the overall beta-elimination of fumarate as a product. The crystal structures of wild-type Escherichia coli ADL (ec-ADL), and mutant-substrate (H171A-ADS) and -product (H171N-AMP.FUM) complexes have been determined to 2.0, 1.85, and 2.0 A resolution, respectively. The H171A-ADS and H171N-AMP.FUM structures provide the first detailed picture of the ADL active site, and have enabled the precise identification of substrate binding and putative catalytic residues. Contrary to previous suggestions, the ec-ADL structures implicate S295 and H171 in base and acid catalysis, respectively. Furthermore, structural alignments of ec-ADL with other superfamily members suggest for the first time a large conformational movement of the flexible C3 loop (residues 287-303) in ec-ADL upon substrate binding and catalysis, resulting in its closure over the active site. This loop movement has been observed in other superfamily enzymes, and has been proposed to be essential for catalysis. The ADL catalytic mechanism is re-examined in light of the results presented here.
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==About this Structure==
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2PTR is a [[Single protein]] structure of 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=2PTR OCA].
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==Reference==
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Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism., Tsai M, Koo J, Yip P, Colman RF, Segall ML, Howell PL, J Mol Biol. 2007 Jul 13;370(3):541-54. Epub 2007 May 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17531264 17531264]
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[[Category: Adenylosuccinate lyase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Howell, P L.]]
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[[Category: Howell PL]]
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[[Category: Tsai, M.]]
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[[Category: Tsai M]]
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[[Category: Adenylosuccinate lyase]]
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[[Category: Mutant-substrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:47:23 2008''
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Current revision

Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171A with bound adenylosuccinate substrate

PDB ID 2ptr

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