1np3

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<StructureSection load='1np3' size='340' side='right'caption='[[1np3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1np3' size='340' side='right'caption='[[1np3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1np3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NP3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1np3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NP3 FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </span></td></tr>
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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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1np3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np3 OCA], [https://pdbe.org/1np3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1np3 RCSB], [https://www.ebi.ac.uk/pdbsum/1np3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1np3 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1np3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np3 OCA], [https://pdbe.org/1np3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1np3 RCSB], [https://www.ebi.ac.uk/pdbsum/1np3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1np3 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ILVC_PSEAE ILVC_PSEAE]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1np3 ConSurf].
</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=1np3 ConSurf].
<div style="clear:both"></div>
<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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Acetohydroxy acid isomeroreductase (AHIR) is a key enzyme in the biosynthesis of branched-chain amino acids. We have determined the first crystal structure of a class I AHIR from Pseudomonas aeruginosa at 2.0 A resolution. Its dodecameric architecture of 23 point group symmetry is assembled of six dimeric units and dimerization is essential for the formation of the active site. The dimeric unit of P.aeruginosa AHIR partially superimposes with a three-domain monomer of spinach AHIR, a class II enzyme. This demonstrates that the so-called plant-specific insert in the middle of spinach AHIR is structurally and functionally equivalent to the C-terminal alpha-helical domain of P.aeruginosa AHIR, and the C-terminal alpha-helical domain was duplicated during evolution from the shorter, class I AHIRs to the longer, class II AHIRs. The dimeric unit of P.aeruginosa AHIR possesses a deep figure-of-eight knot, essentially identical with that in the spinach AHIR monomer. Thus, our work lowers the likelihood of the previous proposal that "domain duplication followed by exchange of a secondary structure element can be a source of such a knot in the protein structure" being correct.
 
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Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa.,Ahn HJ, Eom SJ, Yoon HJ, Lee BI, Cho H, Suh SW J Mol Biol. 2003 Apr 25;328(2):505-15. PMID:12691757<ref>PMID:12691757</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 1np3" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Ketol-acid reductoisomerase 3D structures|Ketol-acid reductoisomerase 3D structures]]
*[[Ketol-acid reductoisomerase 3D structures|Ketol-acid reductoisomerase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ketol-acid reductoisomerase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ahn, H J]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Cho, H]]
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[[Category: Ahn HJ]]
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[[Category: Eom, S J]]
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[[Category: Cho H]]
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[[Category: Lee, B I]]
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[[Category: Eom SJ]]
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[[Category: Suh, S W]]
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[[Category: Lee BI]]
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[[Category: Yoon, H J]]
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[[Category: Suh SW]]
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[[Category: A deep figure-of-eight knot]]
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[[Category: Yoon H-J]]
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[[Category: C-terminal alpha-helical domain]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa

PDB ID 1np3

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