4jo0
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jo0]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4JO0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4jo0]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4JO0 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jo0 OCA], [https://pdbe.org/4jo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jo0 RCSB], [https://www.ebi.ac.uk/pdbsum/4jo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jo0 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=4jo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jo0 OCA], [https://pdbe.org/4jo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jo0 RCSB], [https://www.ebi.ac.uk/pdbsum/4jo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jo0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CMLA_STRVP CMLA_STRVP] Involved in chloramphenicol biosynthesis (PubMed:20713732). Catalyzes the beta-hydroxylation of 4-amino-L-phenylalanine (L-PAPA) covalently bound to CmlP to form L-p-aminophenylserine (PubMed:20713732).<ref>PMID:20713732</ref> | [https://www.uniprot.org/uniprot/CMLA_STRVP CMLA_STRVP] Involved in chloramphenicol biosynthesis (PubMed:20713732). Catalyzes the beta-hydroxylation of 4-amino-L-phenylalanine (L-PAPA) covalently bound to CmlP to form L-p-aminophenylserine (PubMed:20713732).<ref>PMID:20713732</ref> | ||
| - | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4jo0" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal Structure of CmlA, a diiron beta-hydroxylase from Streptomyces venezuelae
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