4jo0

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(Difference between revisions)

Revision as of 11:26, 24 November 2022

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

Structural highlights

4jo0 is a 1 chain structure with sequence from Streptomyces venezuelae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1]

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) Proc. Natl. Acad. Sci. U.S.A. 107, 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-p-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 O2</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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Makris TM, Chakrabarti M, Munck E, Lipscomb JD. A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis. Proc Natl Acad Sci U S A. 2010 Aug 31;107(35):15391-6. doi: , 10.1073/pnas.1007953107. Epub 2010 Aug 16. PMID:20713732 doi:http://dx.doi.org/10.1073/pnas.1007953107
↑ Makris TM, Knoot CJ, Wilmot CM, Lipscomb JD. Structure of a dinuclear iron cluster-containing beta hydroxylase active in antibiotic biosynthesis. Biochemistry. 2013 Aug 27. PMID:23980641 doi:10.1021/bi400845b

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4jo0"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of CmlA, a diiron beta-hydroxylase from Streptomyces venezuelae==
-<StructureSection load='4jo0' size='340' side='right' caption='[[4jo0]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
+<StructureSection load='4jo0' size='340' side='right'caption='[[4jo0]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<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"><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='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='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>
+<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'>[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>
 </table>
+== 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: As 4 1526]]
+[[Category: Large Structures]]
-[[Category: Knoot, C J]]
+[[Category: Streptomyces venezuelae]]
-[[Category: Lipscomb, J D]]
+[[Category: Knoot CJ]]
-[[Category: Makris, T M]]
+[[Category: Lipscomb JD]]
-[[Category: Wilmot, C M]]
+[[Category: Makris TM]]
-[[Category: Antibiotic]]
+[[Category: Wilmot CM]]
-[[Category: Beta-hydroxylation]]
-[[Category: Dinuclear iron cluster]]
-[[Category: Nonheme oxygenase]]
-[[Category: Oxidoreductase]]

4jo0

From Proteopedia

Revision as of 11:26, 24 November 2022

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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