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5msu

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Structure of the R domain of carboxylic acid reductase (CAR) from Mycobacterium marinum in complex with NADP, P21 form

Structural highlights

5msu is a 3 chain structure with sequence from Mycobacterium marinum M. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.74Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAR_MYCMM Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes, by using ATP for energy to drive the reaction. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor.^[1]

Publication Abstract from PubMed

Carboxylic acid reductase (CAR) catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes. The enzyme is related to the nonribosomal peptide synthetases, consisting of an adenylation domain fused via a peptidyl carrier protein (PCP) to a reductase termination domain. Crystal structures of the CAR adenylation-PCP didomain demonstrate that large-scale domain motions occur between the adenylation and thiolation states. Crystal structures of the PCP-reductase didomain reveal that phosphopantetheine binding alters the orientation of a key Asp, resulting in a productive orientation of the bound nicotinamide. This ensures that further reduction of the aldehyde product does not occur. Combining crystallography with small-angle X-ray scattering (SAXS), we propose that molecular interactions between initiation and termination domains are limited to competing PCP docking sites. This theory is supported by the fact that (R)-pantetheine can support CAR activity for mixtures of the isolated domains. Our model suggests directions for further development of CAR as a biocatalyst.

Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis.,Gahloth D, Dunstan MS, Quaglia D, Klumbys E, Lockhart-Cairns MP, Hill AM, Derrington SR, Scrutton NS, Turner NJ, Leys D Nat Chem Biol. 2017 Sep;13(9):975-981. doi: 10.1038/nchembio.2434. Epub 2017 Jul , 17. PMID:28719588^[2]

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

References

↑ Akhtar MK, Turner NJ, Jones PR. Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities. Proc Natl Acad Sci U S A. 2013 Jan 2;110(1):87-92. doi: 10.1073/pnas.1216516110. , Epub 2012 Dec 17. PMID:23248280 doi:http://dx.doi.org/10.1073/pnas.1216516110
↑ Gahloth D, Dunstan MS, Quaglia D, Klumbys E, Lockhart-Cairns MP, Hill AM, Derrington SR, Scrutton NS, Turner NJ, Leys D. Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis. Nat Chem Biol. 2017 Sep;13(9):975-981. doi: 10.1038/nchembio.2434. Epub 2017 Jul , 17. PMID:28719588 doi:http://dx.doi.org/10.1038/nchembio.2434

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/5msu"

Categories: Large Structures | Mycobacterium marinum M | Gahloth D | Leys D

@@ Line 1: / Line 1: @@
 ==Structure of the R domain of carboxylic acid reductase (CAR) from Mycobacterium marinum in complex with NADP, P21 form==
-<StructureSection load='5msu' size='340' side='right' caption='[[5msu]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
+<StructureSection load='5msu' size='340' side='right'caption='[[5msu]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5msu]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MSU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5msu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_marinum_M Mycobacterium marinum M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MSU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.74&#8491;</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=5msu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5msu OCA], [http://pdbe.org/5msu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5msu RCSB], [http://www.ebi.ac.uk/pdbsum/5msu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5msu ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=5msu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5msu OCA], [https://pdbe.org/5msu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5msu RCSB], [https://www.ebi.ac.uk/pdbsum/5msu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5msu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CAR_MYCMM CAR_MYCMM]] Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes, by using ATP for energy to drive the reaction. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor.<ref>PMID:23248280</ref>
+[https://www.uniprot.org/uniprot/CAR_MYCMM CAR_MYCMM] Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes, by using ATP for energy to drive the reaction. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor.<ref>PMID:23248280</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Gahloth, D]]
+[[Category: Large Structures]]
-[[Category: Leys, D]]
+[[Category: Mycobacterium marinum M]]
-[[Category: Adenylation domain]]
+[[Category: Gahloth D]]
-[[Category: Carboxylic acid reductase]]
+[[Category: Leys D]]
-[[Category: Oxidoreductase]]

5msu

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Current revision

Structure of the R domain of carboxylic acid reductase (CAR) from Mycobacterium marinum in complex with NADP, P21 form

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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