Structural and biochemical studies of bacillus subtilis mobb

Dajeong Kim; Sarah Choi; Hyunjin Kim; Jungwoo Choe

doi:10.3390/cryst11101262

Structural and biochemical studies of bacillus subtilis mobb

Dajeong Kim, Sarah Choi, Hyunjin Kim, Jungwoo Choe

Department of Life Science

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

The biosynthesis of molybdenum cofactor for redox enzymes is carried out by multiple enzymes in bacteria including MobA and MobB. MobA is known to catalyze the attachment of GMP to molybdopterin to form molybdopterin guanine dinucleotide. MobB is a GTP binding protein that enhances the activity of MobA by forming the MobA:MobB complex. However, the mechanism of activity enhancement by MobB is not well understood. The structure of Bacillus subtilis MobB was determined to 2.4 Å resolution and it showed an elongated homodimer with an extended β-sheet. Bound sulfate ions were observed in the Walker A motifs, indicating a possible phosphate-binding site for GTP molecules. The binding assay showed that the affinity between B. subtilis MobA and MobB increased in the presence of GTP, suggesting a possible role of MobB as an enhancer of MobA activity.

Original language	English
Article number	1262
Journal	Crystals
Volume	11
Issue number	10
DOIs	https://doi.org/10.3390/cryst11101262
State	Published - Oct 2021

Keywords

Bacillus subtilis
Crystallography
MobB
Molybdenum cofactor
Walker A motif

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10.3390/cryst11101262

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title = "Structural and biochemical studies of bacillus subtilis mobb",

abstract = "The biosynthesis of molybdenum cofactor for redox enzymes is carried out by multiple enzymes in bacteria including MobA and MobB. MobA is known to catalyze the attachment of GMP to molybdopterin to form molybdopterin guanine dinucleotide. MobB is a GTP binding protein that enhances the activity of MobA by forming the MobA:MobB complex. However, the mechanism of activity enhancement by MobB is not well understood. The structure of Bacillus subtilis MobB was determined to 2.4 {\AA} resolution and it showed an elongated homodimer with an extended β-sheet. Bound sulfate ions were observed in the Walker A motifs, indicating a possible phosphate-binding site for GTP molecules. The binding assay showed that the affinity between B. subtilis MobA and MobB increased in the presence of GTP, suggesting a possible role of MobB as an enhancer of MobA activity.",

keywords = "Bacillus subtilis, Crystallography, MobB, Molybdenum cofactor, Walker A motif",

author = "Dajeong Kim and Sarah Choi and Hyunjin Kim and Jungwoo Choe",

note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).",

year = "2021",

month = oct,

doi = "10.3390/cryst11101262",

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T1 - Structural and biochemical studies of bacillus subtilis mobb

AU - Kim, Dajeong

AU - Choi, Sarah

AU - Kim, Hyunjin

AU - Choe, Jungwoo

N1 - Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).

PY - 2021/10

Y1 - 2021/10

N2 - The biosynthesis of molybdenum cofactor for redox enzymes is carried out by multiple enzymes in bacteria including MobA and MobB. MobA is known to catalyze the attachment of GMP to molybdopterin to form molybdopterin guanine dinucleotide. MobB is a GTP binding protein that enhances the activity of MobA by forming the MobA:MobB complex. However, the mechanism of activity enhancement by MobB is not well understood. The structure of Bacillus subtilis MobB was determined to 2.4 Å resolution and it showed an elongated homodimer with an extended β-sheet. Bound sulfate ions were observed in the Walker A motifs, indicating a possible phosphate-binding site for GTP molecules. The binding assay showed that the affinity between B. subtilis MobA and MobB increased in the presence of GTP, suggesting a possible role of MobB as an enhancer of MobA activity.

AB - The biosynthesis of molybdenum cofactor for redox enzymes is carried out by multiple enzymes in bacteria including MobA and MobB. MobA is known to catalyze the attachment of GMP to molybdopterin to form molybdopterin guanine dinucleotide. MobB is a GTP binding protein that enhances the activity of MobA by forming the MobA:MobB complex. However, the mechanism of activity enhancement by MobB is not well understood. The structure of Bacillus subtilis MobB was determined to 2.4 Å resolution and it showed an elongated homodimer with an extended β-sheet. Bound sulfate ions were observed in the Walker A motifs, indicating a possible phosphate-binding site for GTP molecules. The binding assay showed that the affinity between B. subtilis MobA and MobB increased in the presence of GTP, suggesting a possible role of MobB as an enhancer of MobA activity.

KW - Bacillus subtilis

KW - Crystallography

KW - MobB

KW - Molybdenum cofactor

KW - Walker A motif

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U2 - 10.3390/cryst11101262

DO - 10.3390/cryst11101262

M3 - Article

AN - SCOPUS:85118218222

SN - 2073-4352

VL - 11

JO - Crystals

JF - Crystals

IS - 10

M1 - 1262

ER -

Structural and biochemical studies of bacillus subtilis mobb

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