This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4n5l

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase from Ralstonia eutropha

Structural highlights

4n5l is a 2 chain structure with sequence from Cupriavidus necator H16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.65Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHAB_CUPNH Catalyzes the chiral reduction of acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA. Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

(R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha H16 (RePhaB) is an enzyme that catalyzes the NADPH-dependent reduction of acetoacetyl-CoA, an intermediate of polyhydroxyalkanoates (PHA) synthetic pathways. Polymeric PHA is used to make bioplastics, implant biomaterials, and biofuels. Here, we report the crystal structures of RePhaB apoenzyme and in complex with either NADP+ or acetoacetyl-CoA, which provide the catalytic mechanism of the protein. RePhaB contains a Rossmann fold and a Clamp domain for binding of NADP+ and acetoacetyl-CoA, respectively. The NADP+-bound form of RePhaB structure reveals that the protein has a unique cofactor binding mode. Interestingly, in the RePhaB structure in complex with acetoacetyl-CoA, the conformation of the Clamp domain, especially the Clamp-lid, undergoes a large structural change about 4.6A leading to formation of the substrate pocket. These structural observations, along with the biochemical experiments, suggest that movement of the Clamp-lid enables the substrate binding and ensures the acetoacetyl moiety is located near to the nicotinamide ring of NADP+.

Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha.,Kim J, Chang JH, Kim EJ, Kim KJ Biochem Biophys Res Commun. 2013 Nov 6. pii: S0006-291X(13)01843-3. doi:, 10.1016/j.bbrc.2013.10.150. PMID:24211201^[5]

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

References

↑ Matsumoto K, Tanaka Y, Watanabe T, Motohashi R, Ikeda K, Tobitani K, Yao M, Tanaka I, Taguchi S. Directed evolution and structural analysis of NADPH-dependent acetoacetyl-CoA reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics. Appl Environ Microbiol. 2013 Aug 2. PMID:23913421 doi:10.1128/AEM.01768-13
↑ Kim J, Chang JH, Kim EJ, Kim KJ. Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha. Biochem Biophys Res Commun. 2013 Nov 6. pii: S0006-291X(13)01843-3. doi:, 10.1016/j.bbrc.2013.10.150. PMID:24211201 doi:http://dx.doi.org/10.1016/j.bbrc.2013.10.150
↑ Peoples OP, Sinskey AJ. Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase. J Biol Chem. 1989 Sep 15;264(26):15293-7. PMID:2670935
↑ Peoples OP, Sinskey AJ. Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC). J Biol Chem. 1989 Sep 15;264(26):15298-303. PMID:2670936
↑ Kim J, Chang JH, Kim EJ, Kim KJ. Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha. Biochem Biophys Res Commun. 2013 Nov 6. pii: S0006-291X(13)01843-3. doi:, 10.1016/j.bbrc.2013.10.150. PMID:24211201 doi:http://dx.doi.org/10.1016/j.bbrc.2013.10.150

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/4n5l"

Categories: Cupriavidus necator H16 | Large Structures | Kim J-E | Kim K-J | Kim S

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4n5l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator_H16 Cupriavidus necator H16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N5L FirstGlance]. <br>
-</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=4n5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5l OCA], [https://pdbe.org/4n5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n5l RCSB], [https://www.ebi.ac.uk/pdbsum/4n5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n5l ProSAT]</span></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]] 1.65&#8491;</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=4n5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5l OCA], [https://pdbe.org/4n5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n5l RCSB], [https://www.ebi.ac.uk/pdbsum/4n5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n5l ProSAT]</span></td></tr>
 </table>
 == Function ==

4n5l

From Proteopedia

Current revision

Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase from Ralstonia eutropha

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox