4jo0

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==Crystal Structure of CmlA, a diiron beta-hydroxylase from Streptomyces venezuelae==
==Crystal Structure of CmlA, a diiron beta-hydroxylase from Streptomyces venezuelae==
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<StructureSection load='4jo0' size='340' side='right' caption='[[4jo0]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
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<StructureSection load='4jo0' size='340' side='right'caption='[[4jo0]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4jo0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1526 As 4.1526]. 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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
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<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 AS 4.1526])</td></tr>
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<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>
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<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://pdbe.org/4jo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jo0 RCSB], [http://www.ebi.ac.uk/pdbsum/4jo0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jo0 ProSAT]</span></td></tr>
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<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>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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>
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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) &lt;i&gt;Proc. Natl. Acad. Sci. U.S.A. 107&lt;/i&gt;, 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-&lt;i&gt;p&lt;/i&gt;-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&lt;sub&gt;2&lt;/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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4jo0" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: As 4 1526]]
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[[Category: Large Structures]]
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[[Category: Knoot, C J]]
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[[Category: Streptomyces venezuelae]]
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[[Category: Lipscomb, J D]]
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[[Category: Knoot CJ]]
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[[Category: Makris, T M]]
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[[Category: Lipscomb JD]]
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[[Category: Wilmot, C M]]
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[[Category: Makris TM]]
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[[Category: Antibiotic]]
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[[Category: Wilmot CM]]
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[[Category: Beta-hydroxylation]]
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[[Category: Dinuclear iron cluster]]
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[[Category: Nonheme oxygenase]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of CmlA, a diiron beta-hydroxylase from Streptomyces venezuelae

PDB ID 4jo0

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