6lnh: Difference between revisions

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

↑ 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
↑ 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
↑ 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

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OCA

[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

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6lnh is ON HOLD
+==Crystal structure of IDO from Bacillus thuringiensis==
+<StructureSection load='6lnh' size='340' side='right'caption='[[6lnh]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<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>
-Description:
+</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>
-[[Category: Unreleased Structures]]
+<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>
+== 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__
+</StructureSection>
+[[Category: Bacillus thuringiensis]]
+[[Category: Large Structures]]
+[[Category: Chen CC]]
+[[Category: Feng Y]]
+[[Category: Guo RT]]
+[[Category: Huang JW]]
+[[Category: Liu WD]]

6lnh: Difference between revisions

Latest revision as of 12:15, 25 October 2023

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

Structural highlights

Function

References

Contents

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6lnh: Difference between revisions

Latest revision as of 12:15, 25 October 2023

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

Structural highlights

Function

References

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