PDBsum entry: 1ckv

Hydroxylase regulatory protein

PDB id: 1ckv

Contents

Protein chain

141 a.a. *

* Residue conservation analysis

PDB id:

1ckv

Name:

Hydroxylase regulatory protein

Title:

Structure of the soluble methane monooxygenase regulatory protein b

Structure:

Protein (protein b). Chain: a

Source:

Escherichia coli. Organism_taxid: 562

NMR struc:

14 models

Authors:

K.J.Walters,G.T.Gassner,S.J.Lippard,G.Wagner

Key ref:

K.J.Walters et al. (1999). Structure of the soluble methane monooxygenase regulatory protein B. Proc Natl Acad Sci U S A, 96, 7877-7882. PubMed id: 10393915 DOI: 10.1073/pnas.96.14.7877

Date:

25-Apr-99 Release date: 07-Jul-99

Protein chain

P18797  (MMOB_METCA) -  Methane monooxygenase regulatory protein B

Seq: 141 a.a.

Struc: 141 a.a.

 Gene Ontology (GO) functional annotation 

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

DOI no: 10.1073/pnas.96.14.7877

Proc Natl Acad Sci U S A 96:7877-7882 (1999)

PubMed id: 10393915

Structure of the soluble methane monooxygenase regulatory protein B.

K.J.Walters, G.T.Gassner, S.J.Lippard, G.Wagner.

ABSTRACT

The soluble methane monooxygenase (sMMO; EC 1.14.13.25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enzyme system that catalyzes the selective oxidation of methane to methanol. We have used NMR spectroscopy to produce a highly refined structure of MMOB, the 16-kDa regulatory protein of this system. This structure has a unique and intricate fold containing seven beta-strands forming two beta-sheets oriented perpendicular to each other and bridged by three alpha-helices. The rate and efficiency of the methane hydroxylation by sMMO depend on dynamic binding interactions of the hydroxylase with the reductase and regulatory protein components during catalysis. We have monitored by NMR the binding of MMOB to the hydroxylase in the presence and absence of the reductase. The results of these studies provide structural insight into how the regulatory protein interacts with the hydroxylase.

Selected figure(s)

Figure 1.
Fig. 1. Line shape simulations of MMOB titrations with MMOH by using Eq. 5 and k[off] values of 3.2 s^ 1 (A) or 25.6 s^ 1 (B) for chemical shift differences of 0 Hz (black) and 500 Hz (red). R[1], R[2], and a are 23 Hz, 250 Hz, and 0.8, respectively. In C is presented a comparison of observed peak height differences from [^15N,^1H]-HSQC spectra of MMOB in the absence of hydroxylase and at a 10 MMOB to 1 MMOH ratio. Differences are normalized according to Eq. 6, and the homology conservation color scheme of Fig. 3 is used to highlight the correlation between sequence conservation and binding data.

Figure 5.
Fig. 5. A surface diagram model for docking MMOB (top) into the canyon of MMOH (bottom). Each subunit of MMOH is distinguished by color, whereas MMOB is colored according to our binding data. Residues of MMOB most affected by binding are colored blue and those least affected are red. For clarity, MMOB has been translated away from its proposed docking site on the surface of the hydroxylase and rotated clockwise about the y-axis by 90° to expose residues most involved in binding. This figure was produced by using GRASP (29).

Figures were selected by an automated process.