2gv1

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{{Seed}}
 
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[[Image:2gv1.png|left|200px]]
 
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==NMR solution structure of the Acylphosphatase from Eschaerichia Coli==
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The line below this paragraph, containing "STRUCTURE_2gv1", creates the "Structure Box" on the page.
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<StructureSection load='2gv1' size='340' side='right'caption='[[2gv1]]' 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'>[[2gv1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GV1 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">Solution NMR, 20 models</td></tr>
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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=2gv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gv1 OCA], [https://pdbe.org/2gv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gv1 RCSB], [https://www.ebi.ac.uk/pdbsum/2gv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gv1 ProSAT]</span></td></tr>
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{{STRUCTURE_2gv1| PDB=2gv1 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACYP_ECOLI ACYP_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/gv/2gv1_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=2gv1 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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The solution structure of Escherichia coli acylphosphatase (E. coli AcP), a small enzyme catalyzing the hydrolysis of acylphosphates, was determined by (1)H and (15)N NMR and restrained modelling calculation. In analogy with the other members of AcP family, E. coli AcP shows an alpha/beta sandwich domain composed of four antiparallel and one parallel beta-strand, assembled in a five-stranded beta-sheet facing two antiparallel alpha-helices. The pairwise RMSD values calculated for the backbone atoms of E. coli and Sulfolobus solfataricus AcP, Bovine common type AcP and Horse muscle AcP are 2.18, 5.31 and 5.12 A, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures.
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===NMR solution structure of the Acylphosphatase from Eschaerichia Coli===
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NMR solution structure of the acylphosphatase from Escherichia coli.,Pagano K, Ramazzotti M, Viglino P, Esposito G, Degl'Innocenti D, Taddei N, Corazza A J Biomol NMR. 2006 Nov;36(3):199-204. Epub 2006 Oct 5. PMID:17021943<ref>PMID:17021943</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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The line below this paragraph, {{ABSTRACT_PUBMED_17021943}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2gv1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17021943 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17021943}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2GV1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GV1 OCA].
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==Reference==
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NMR solution structure of the acylphosphatase from Escherichia coli., Pagano K, Ramazzotti M, Viglino P, Esposito G, Degl'Innocenti D, Taddei N, Corazza A, J Biomol NMR. 2006 Nov;36(3):199-204. Epub 2006 Oct 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17021943 17021943]
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Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus., Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P, Proteins. 2006 Jan 1;62(1):64-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16287076 16287076]
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Crystal structure of common type acylphosphatase from bovine testis., Thunnissen MM, Taddei N, Liguri G, Ramponi G, Nordlund P, Structure. 1997 Jan 15;5(1):69-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9016712 9016712]
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Three-dimensional structure of acylphosphatase. Refinement and structure analysis., Pastore A, Saudek V, Ramponi G, Williams RJ, J Mol Biol. 1992 Mar 20;224(2):427-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1313885 1313885]
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[[Category: Acylphosphatase]]
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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: Corazza, A.]]
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[[Category: Corazza A]]
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[[Category: Esposito, G.]]
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[[Category: Esposito G]]
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[[Category: Pagano, K.]]
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[[Category: Pagano K]]
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[[Category: Viglino, P.]]
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[[Category: Viglino P]]
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[[Category: Globular alpha-helix/beta-sheet protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:54:40 2008''
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Current revision

NMR solution structure of the Acylphosphatase from Eschaerichia Coli

PDB ID 2gv1

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