Insight into the sporulation phosphorelay: Crystal structure of the sensor domain of Bacillus subtilis
 histidine kinase, KinD

ABSTRACT A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.

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Crystal structure of heme A synthase from Bacillus subtilis

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1813346115 ◽

2018 ◽

Vol 115 (47) ◽

pp. 11953-11957 ◽

Cited By ~ 5

Author(s):

Satomi Niwa ◽

Kazuki Takeda ◽

Masayuki Kosugi ◽

Erika Tsutsumi ◽

Tatsushi Mogi ◽

...

Keyword(s):

Crystal Structure ◽

Bacillus Subtilis ◽

Transmembrane Helix ◽

Integral Membrane Protein ◽

Heme Binding ◽

Terminal Oxidases ◽

Domain Structures ◽

Heme A Synthase ◽

Insight Into ◽

Heme Molecule

Heme A is an essential cofactor for respiratory terminal oxidases and vital for respiration in aerobic organisms. The final step of heme A biosynthesis is formylation of the C-8 methyl group of heme molecule by heme A synthase (HAS). HAS is a heme-containing integral membrane protein, and its structure and reaction mechanisms have remained unknown. Thus, little is known about HAS despite of its importance. Here we report the crystal structure of HAS from Bacillus subtilis at 2.2-Å resolution. The N- and C-terminal halves of HAS consist of four-helix bundles and they align in a pseudo twofold symmetry manner. Each bundle contains a pair of histidine residues and forms a heme-binding domain. The C-half domain binds a cofactor-heme molecule, while the N-half domain is vacant. Many water molecules are found in the transmembrane region and around the substrate-binding site, and some of them interact with the main chain of transmembrane helix. Comparison of these two domain structures enables us to construct a substrate-heme binding state structure. This structure implies that a completely conserved glutamate, Glu57 in B. subtilis, is the catalytic residue for the formylation reaction. These results provide valuable suggestions of the substrate-heme binding mechanism. Our results present significant insight into the heme A biosynthesis.

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The Crystal Structure of Bacillus subtilis YycI Reveals a Common Fold for Two Members of an Unusual Class of Sensor Histidine Kinase Regulatory Proteins

Journal of Bacteriology ◽

10.1128/jb.01937-06 ◽

2007 ◽

Vol 189 (8) ◽

pp. 3290-3295 ◽

Cited By ~ 23

Author(s):

Eugenio Santelli ◽

Robert C. Liddington ◽

Michael A. Mohan ◽

James A. Hoch ◽

Hendrik Szurmant

Keyword(s):

Crystal Structure ◽

Bacillus Subtilis ◽

Sequence Homology ◽

Histidine Kinase ◽

Direct Interaction ◽

Regulatory Proteins ◽

Sensor Histidine Kinase ◽

Periplasmic Proteins ◽

Terminal Domains

ABSTRACT YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-Å resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins.

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Faculty Opinions recommendation of Crystal structure of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Bacillus subtilis.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1014168.192837 ◽

2003 ◽

Author(s):

Haruo Seto

Keyword(s):

Crystal Structure ◽

Bacillus Subtilis ◽

Type Ii

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Faculty Opinions recommendation of Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.11917958.13033056 ◽

2011 ◽

Author(s):

Berl R Oakley

Keyword(s):

Crystal Structure ◽

Microtubule Nucleation ◽

Complex Protein ◽

Insight Into

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Crystal structure of KBSi3O8 isostructural with danburite

Mineralogical Magazine ◽

10.1180/minmag.1993.057.386.15 ◽

1993 ◽

Vol 57 (386) ◽

pp. 157-164 ◽

Cited By ~ 14

Author(s):

Mitsuyoshi Kimata

Keyword(s):

Crystal Structure ◽

Direct Method ◽

Crystal Chemical ◽

Chemical Formula ◽

Crystal Chemical Formula ◽

3 Dimensional ◽

Tetrahedral Sites ◽

Structural Types ◽

Coupled Substitution ◽

Insight Into

AbstractThe crystal structure of KBSi3O8 (orthorhombic, Pnam, with a = 8.683(1), b = 9.253(1), c = 8.272(1) Å,, V = 664.4(1) Å3, Z = 4) has been determined by the direct method applied to 3- dimensional rcflection data. The structure of a microcrystal with the dimensions 20 × 29 × 37 μm was refined to an unweightcd residual of R = 0.031 using 386 non-zero structure amplitudes. KBSi3O8 adopts a structure essentially different from recdmergneritc NaBSi3O8, with the low albite (NaAlSi3O8) structure, and isotypic with danburite CaB2Si2Os which has the same topology as paracelsian BaAl2Si2O8. The chenfical relationship between this sample and danburitc gives insight into a new coupled substitution; K+ + Si4+ = Ca2+ + B3+ in the extraframework and tetrahedral sites. The present occupancy refinement revealed partial disordering of B and Si atoms which jointly reside in two kinds of general equivalent points, T(1) and T(2) sites. Thus the expanded crystal-chemical formula can be written in the form K(B0.44Si0.56)2(B0.06Si0.94)2O8The systematic trend among crystalline compounds with the M+T3+T4+3O8 formula suggests that they exist in one of four structural types; the feldspar structures with T3+/T4+ ordered and/or disordered forms, and the paracelsian and the hollandite structures.

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