6lnh: Difference between revisions

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==Crystal structure of IDO from Bacillus thuringiensis==
==Crystal structure of IDO from Bacillus thuringiensis==
<StructureSection load='6lnh' size='340' side='right'caption='[[6lnh]]' scene=''>
<StructureSection load='6lnh' size='340' side='right'caption='[[6lnh]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LNH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LNH FirstGlance]. <br>
<table><tr><td colspan='2'>[[6lnh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LNH FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnh OCA], [http://pdbe.org/6lnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lnh RCSB], [http://www.ebi.ac.uk/pdbsum/6lnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnh ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=6lnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnh OCA], [https://pdbe.org/6lnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lnh RCSB], [https://www.ebi.ac.uk/pdbsum/6lnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IDO_BACTU IDO_BACTU] Catalyzes the hydroxylation of L-isoleucine to produce (4S)-4-hydroxy-L-isoleucine (PubMed:20665018, PubMed:19850012, PubMed:21821743). Can also catalyze the hydroxylation of L-leucine, L-norvaline, L-norleucine and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine (PubMed:21821743).<ref>PMID:19850012</ref> <ref>PMID:20665018</ref> <ref>PMID:21821743</ref>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus thuringiensis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen CC]]
[[Category: Chen CC]]

Latest revision as of 12:15, 25 October 2023

Crystal structure of IDO from Bacillus thuringiensisCrystal structure of IDO from Bacillus thuringiensis

Structural highlights

6lnh is a 4 chain structure with sequence from Bacillus thuringiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.34Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IDO_BACTU Catalyzes the hydroxylation of L-isoleucine to produce (4S)-4-hydroxy-L-isoleucine (PubMed:20665018, PubMed:19850012, PubMed:21821743). Can also catalyze the hydroxylation of L-leucine, L-norvaline, L-norleucine and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine (PubMed:21821743).[1] [2] [3]

References

  1. Kodera T, Smirnov SV, Samsonova NN, Kozlov YI, Koyama R, Hibi M, Ogawa J, Yokozeki K, Shimizu S. A novel l-isoleucine hydroxylating enzyme, l-isoleucine dioxygenase from Bacillus thuringiensis, produces (2S,3R,4S)-4-hydroxyisoleucine. Biochem Biophys Res Commun. 2009 Dec 18;390(3):506-10. PMID:19850012 doi:10.1016/j.bbrc.2009.09.126
  2. Smirnov SV, Kodera T, Samsonova NN, Kotlyarova VA, Rushkevich NY, Kivero AD, Sokolov PM, Hibi M, Ogawa J, Shimizu S. Metabolic engineering of Escherichia coli to produce (2S, 3R, 4S)-4-hydroxyisoleucine. Appl Microbiol Biotechnol. 2010 Oct;88(3):719-26. PMID:20665018 doi:10.1007/s00253-010-2772-3
  3. Hibi M, Kawashima T, Kodera T, Smirnov SV, Sokolov PM, Sugiyama M, Shimizu S, Yokozeki K, Ogawa J. Characterization of Bacillus thuringiensis L-isoleucine dioxygenase for production of useful amino acids. Appl Environ Microbiol. 2011 Oct;77(19):6926-30. PMID:21821743 doi:10.1128/AEM.05035-11

6lnh, resolution 2.34Å

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