PDBsum entry: 1bsl

Flavoprotein

PDB id: 1bsl

Contents

Protein chains

323 a.a. *

Waters ×989

* Residue conservation analysis

PDB id:

1bsl

Name:

Flavoprotein

Title:

Structure of alkanal monooxygenase beta chain

Structure:

Bacterial luciferase. Chain: a, b. Fragment: beta subunit. Engineered: yes

Source:

Vibrio harveyi. Organism_taxid: 669. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Hetero-Dimer (from PDB file)

Resolution:

1.95Å R-factor: 0.188

Authors:

I.Rayment,H.M.Holden,J.B.Thoden,T.O.Baldwin

Key ref:

J.B.Thoden et al. (1997). Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap. Protein Sci, 6, 13-23. PubMed id: 9007973 Ref: Full text

Date:

22-Oct-96 Release date: 12-Nov-97

Protein chains

P07739  (LUXB_VIBHA) -  Alkanal monooxygenase beta chain

Seq: 324 a.a.

Struc: 323 a.a.

Enzyme reactions

• Enzyme class: E.C.1.14.14.3 - Alkanal monooxygenase (FMN-linked).
• Reaction: RCHO + reduced FMN + O₂ = RCOOH + FMN + H₂O + light

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: oxidation-reduction process (2 terms)
• Biochemical function: oxidoreductase activity (4 terms)

reference

Full text	Protein Sci 6:13-23 (1997)
PubMed id: 9007973

Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap.

J.B.Thoden, H.M.Holden, A.J.Fisher, J.F.Sinclair, G.Wesenberg, T.O.Baldwin, I.Rayment.

ABSTRACT

Luciferase, as isolated from Vibrio harveyi, is an alpha beta heterodimer. When allowed to fold in the absence of the alpha subunit, either in vitro or in vivo, the beta subunit of enzyme will form a kinetically stable homodimer that does not unfold even after prolonged incubation in 5 M urea at pH 7.0 and 18 degrees C. This form of the beta subunit, arising via kinetic partitioning on the folding pathway, appears to constitute a kinetically trapped alternative to the heterodimeric enzyme (Sinclair JF, Ziegler MM, Baldwin TO. 1994. Kinetic partitioning during protein folding yields multiple native states. Nature Struct Biol 1: 320-326). Here we describe the X-ray crystal structure of the beta 2 homodimer of luciferase from V. harveyi determined and refined at 1.95 A resolution. Crystals employed in the investigational belonged to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of a = 58.8 A, b = 62.0 A, and c = 218.2 A and contained one dimer per asymmetric unit. Like that observed in the functional luciferase alpha beta heterodimer, the major tertiary structural motif of each beta subunit consists of an (alpha/beta)8 barrel (Fisher AJ, Raushel FM, Baldwin TO, Rayment I. 1995. Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 A resolution. Biochemistry 34: 6581-6586). The root-mean-square deviation of the alpha-carbon coordinates between the beta subunits of the hetero- and homodimers is 0.7 A. This high resolution X-ray analysis demonstrated that "domain" or "loop" swapping has not occurred upon formation of the beta 2 homodimer and thus the stability of the beta 2 species to denaturation cannot be explained in such simple terms. In fact, the subunit:subunit interfaces observed in both the beta 2 homodimer and alpha beta heterodimer are remarkably similar in hydrogen-bonding patterns and buried surface areas.

Selected figure(s)

Figure 1.
Fig. 1. Ribbon representation f the P2 homodimer of bacterial luciferase. Subunit 1 shown in lueand green while Subunit 2 is depicted in red and he local two-fold rotational axis relating thetwo subunits in the dimer is located at the enter of the igure and lying perpendicular to the plane of the page. hesubunitmbunit interface is formed by amino residues residing in primarily a-helical regions. Thefour surface loops that differ n conformation between the two subunits are shown in white, whereas the putative vestigial active site for Subunit 1 liesat the C-terminal end of -barrel is indicated by the arrow. Figures 1-4 were prepared with the program MOLSCRIPT(Kraulis, 1991).

Figure 4.
Fig. 4. Close-upview of theburiedwatermoleculethat lie attheinterface of the ap heterodimerand p2 homoimer.a-carbons 10 to 165 are shown.Thewaterpocket is locatedabove thefourhlixbundlethat forms thecore of theprotein-proteininterface. A: ap hterodimerwherethe a and p subunitsaredepictedinredandblue,respectively. B: p2 omodimerwhereSubunits 1 nd 2 are shown in redand blue,respectively. B also marksthelocation of heidenticalresidues in thesequences of the a and p subunitas small spheres.

The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (1997, 6, 13-23) copyright 1997.

Figures were selected by an automated process.