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==Crystal Structure of CmlA, a diiron beta-hydroxylase from Streptomyces venezuelae== | |||
<StructureSection load='4jo0' size='340' side='right' caption='[[4jo0]], [[Resolution|resolution]] 2.17Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jo0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JO0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CMLA, SVEN_0921 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54571 Streptomyces venezuelae])</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=4jo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jo0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jo0 RCSB], [http://www.ebi.ac.uk/pdbsum/4jo0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A family of dinuclear iron cluster-containing oxygenases was recently described that catalyze beta-hydroxylation tailoring reactions in natural product biosynthesis by nonribosomal peptide synthetase (NRPS) systems (Makris, T. M., Chakrabarti, M., Munck, E., and Lipscomb, J. D. (2010) <i>Proc. Natl. Acad. Sci. U.S.A. 107</i>, 15391-15396). Here, the 2.17 A X-ray crystal structure of the archetypal enzyme from the family, CmlA, is reported. CmlA catalyzes beta-hydroxylation of L-<i>p</i>-aminophenylalanine during chloramphenicol biosynthesis. The fold of the N-terminal domain of CmlA is unlike any previously reported, but the C-terminal domain has the alphabetabetaalpha-fold of the metallo-beta-lactamase (MBL) superfamily. The diiron cluster bound in the C-terminal domain is coordinated by an acetate, three His, two Asp, one Glu and a bridging oxo moiety. One of the Asp ligands forms an unusual monodentate bridge. No other oxygen-activating diiron enzyme utilizes this ligation or the MBL protein fold. The N-terminal domain facilitates dimerization, but using computational docking and a sequence-based structural comparison to homologs, we hypothesize that it likely serves additional roles in NRPS recognition and the regulation of O<sub>2</sub activation. | |||
Structure of a dinuclear iron cluster-containing beta hydroxylase active in antibiotic biosynthesis.,Makris TM, Knoot CJ, Wilmot CM, Lipscomb JD Biochemistry. 2013 Aug 27. PMID:23980641<ref>PMID:23980641</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Streptomyces venezuelae]] | [[Category: Streptomyces venezuelae]] | ||
[[Category: Knoot, C J | [[Category: Knoot, C J]] | ||
[[Category: Lipscomb, J D | [[Category: Lipscomb, J D]] | ||
[[Category: Makris, T M | [[Category: Makris, T M]] | ||
[[Category: Wilmot, C M | [[Category: Wilmot, C M]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
[[Category: Beta-hydroxylation]] | [[Category: Beta-hydroxylation]] | ||
Revision as of 14:41, 21 December 2014
Crystal Structure of CmlA, a diiron beta-hydroxylase from Streptomyces venezuelae
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