1f2d

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{{Seed}}
 
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[[Image:1f2d.png|left|200px]]
 
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==1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE==
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The line below this paragraph, containing "STRUCTURE_1f2d", creates the "Structure Box" on the page.
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<StructureSection load='1f2d' size='340' side='right'caption='[[1f2d]], [[Resolution|resolution]] 2.00&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'>[[1f2d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyberlindnera_saturnus Cyberlindnera saturnus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2D 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]] 2&#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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1f2d| PDB=1f2d | 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=1f2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2d OCA], [https://pdbe.org/1f2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2d RCSB], [https://www.ebi.ac.uk/pdbsum/1f2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/1A1D_CYBSA 1A1D_CYBSA] Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate.
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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/f2/1f2d_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=1f2d 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 pyridoxal 5'-phosphate (PLP)-dependent enzyme 1-aminocyclopropane-1-carboxylate deaminase (ACCD) catalyzes a reaction that involves a ring opening of cyclopropanoid amino acid, yielding alpha-ketobutyrate and ammonia. Unlike other PLP-dependent enzymes, this enzyme has no alpha-hydrogen atom in the substrate. Thus, a unique mechanism for the bond cleavage is expected. The crystal structure of ACCD from Hansenula saturnus has been determined at 2.0 A resolution by the multiple wavelength anomalous diffraction method using mercury atoms as anomalous scatterers. The model was built on the electron density map, which was obtained by the density averaging of multiple crystal forms. The final model was refined to an R-factor of 22.5% and an R(free)-factor of 26.8%. The ACCD folds into two domains, each of which has an open twisted alpha/beta structure similar to the beta-subunit of tryptophan synthase. However, in ACCD, unlike in other members of the beta family of PLP-dependent enzymes, PLP is buried deep in the molecule. The structure provides the first view of the catalytic center of the cyclopropane ring opening.
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===1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE===
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Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus.,Yao M, Ose T, Sugimoto H, Horiuchi A, Nakagawa A, Wakatsuki S, Yokoi D, Murakami T, Honma M, Tanaka I J Biol Chem. 2000 Nov 3;275(44):34557-65. PMID:10938279<ref>PMID:10938279</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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<div class="pdbe-citations 1f2d" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10938279}}, adds the Publication Abstract to the page
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*[[Deaminase 3D structures|Deaminase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10938279 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10938279}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Cyberlindnera saturnus]]
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1F2D is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Williopsis_saturnus Williopsis saturnus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2D OCA].
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[[Category: Large Structures]]
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[[Category: Honma M]]
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==Reference==
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[[Category: Horiuchi A]]
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<ref group="xtra">PMID:10938279</ref><references group="xtra"/>
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[[Category: Murakami T]]
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[[Category: 1-aminocyclopropane-1-carboxylate deaminase]]
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[[Category: Nakagawa A]]
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[[Category: Williopsis saturnus]]
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[[Category: Ose T]]
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[[Category: Honma, M.]]
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[[Category: Sugimoto H]]
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[[Category: Horiuchi, A.]]
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[[Category: Tanaka I]]
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[[Category: Murakami, T.]]
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[[Category: Wakatsuki S]]
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[[Category: Nakagawa, A.]]
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[[Category: Yao M]]
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[[Category: Ose, T.]]
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[[Category: Yokoi D]]
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[[Category: Sugimoto, H.]]
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[[Category: Tanaka, I.]]
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[[Category: Wakatsuki, S.]]
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[[Category: Yao, M.]]
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[[Category: Yokoi, D.]]
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[[Category: Carbon-carbon lyase]]
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[[Category: Open twisted alpha/beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 05:34:40 2009''
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Current revision

1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE

PDB ID 1f2d

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