5aec: Difference between revisions
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''' | ==Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.== | ||
<StructureSection load='5aec' size='340' side='right' caption='[[5aec]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5aec]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wgk 2wgk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AEC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PIN:PIPERAZINE-N,N-BIS(2-ETHANESULFONIC+ACID)'>PIN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<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=5aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5aec RCSB], [http://www.ebi.ac.uk/pdbsum/5aec PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/C16MO_PSEPU C16MO_PSEPU]] Involved in the degradation of (-)-camphor. Catalyzes the lactonization of the 3,6-diketocamphane via the Baeyer-Villiger oxidation to produce the unstable lactone (-)-5-oxo-1,2-campholide that presumably undergoes spontaneous hydrolysis to form 2-oxo-delta(3)-4,5,5-trimethylcyclopentenylacetic acid. It acts only on bicyclic ketones.<ref>PMID:22286514</ref> <ref>PMID:8515237</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The efficiency of the cross-rotation function step of molecular replacement (MR) is intrinsically limited as it uses only a fraction of the Patterson vectors. Along with general techniques extending the boundaries of the method, there are approaches that utilize specific features of a given structure. In special cases, where the directions of noncrystallographic symmetry axes can be unambiguously derived from the self-rotation function and the structure of the homologue protein is available in a related oligomeric state, the cross-rotation function step of MR can be omitted. In such cases, a small number of yet unknown parameters defining the orientation of the oligomer and/or its internal organization can be optimized using an exhaustive search. Three difficult MR cases are reported in which these parameters were determined and the oligomer was positioned according to the maximal value of the correlation coefficient in a series of translation searches. | |||
NCS-constrained exhaustive search using oligomeric models.,Isupov MN, Lebedev AA Acta Crystallogr D Biol Crystallogr. 2008 Jan;64(Pt 1):90-8. Epub 2007 Dec 5. PMID:18094472<ref>PMID:18094472</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Beecher, J]] | |||
[[Category: Bornscheuer, U T]] | |||
[[Category: Bourenkov, G]] | |||
[[Category: Davenport, C F]] | |||
[[Category: Dcunha, S]] | |||
[[Category: Donadio, G]] | [[Category: Donadio, G]] | ||
[[Category: | [[Category: Gibson, R P]] | ||
[[Category: Hasegawa, Y]] | [[Category: Hasegawa, Y]] | ||
[[Category: | [[Category: Isupov, M N]] | ||
[[Category: Iwaki, H]] | [[Category: Iwaki, H]] | ||
[[Category: Kadow, M]] | |||
[[Category: Lau, P C]] | |||
[[Category: Littlechild, J A]] | |||
[[Category: Loschinski, K]] | [[Category: Loschinski, K]] | ||
[[Category: McGhie, E J]] | |||
[[Category: Saneei, V]] | |||
[[Category: Sayer, C]] | |||
[[Category: Schroeder, E]] | [[Category: Schroeder, E]] | ||
[[Category: | [[Category: Biocatalysis]] | ||
[[Category: | [[Category: Flavin monooxygenase]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
Revision as of 14:06, 9 September 2015
Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.
Structural highlights
Function[C16MO_PSEPU] Involved in the degradation of (-)-camphor. Catalyzes the lactonization of the 3,6-diketocamphane via the Baeyer-Villiger oxidation to produce the unstable lactone (-)-5-oxo-1,2-campholide that presumably undergoes spontaneous hydrolysis to form 2-oxo-delta(3)-4,5,5-trimethylcyclopentenylacetic acid. It acts only on bicyclic ketones.[1] [2] Publication Abstract from PubMedThe efficiency of the cross-rotation function step of molecular replacement (MR) is intrinsically limited as it uses only a fraction of the Patterson vectors. Along with general techniques extending the boundaries of the method, there are approaches that utilize specific features of a given structure. In special cases, where the directions of noncrystallographic symmetry axes can be unambiguously derived from the self-rotation function and the structure of the homologue protein is available in a related oligomeric state, the cross-rotation function step of MR can be omitted. In such cases, a small number of yet unknown parameters defining the orientation of the oligomer and/or its internal organization can be optimized using an exhaustive search. Three difficult MR cases are reported in which these parameters were determined and the oligomer was positioned according to the maximal value of the correlation coefficient in a series of translation searches. NCS-constrained exhaustive search using oligomeric models.,Isupov MN, Lebedev AA Acta Crystallogr D Biol Crystallogr. 2008 Jan;64(Pt 1):90-8. Epub 2007 Dec 5. PMID:18094472[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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