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Crystallization and preliminary X-ray crystallographic analysis of MinE, the cell-division topological specificity factor from Helicobacter pylori.

ABSTRACT: Cell division in Gram-negative bacteria is driven by the formation of an FtsZ ring at the division site. MinE regulates the proper placement of the FtsZ ring at mid-cell by blocking the inhibitory action of the MinCD complex. Diffraction data were collected at 2.8 A resolution from a native crystal of full-length Helicobacter pylori MinE. The crystal belonged to space group P6(4). Assuming the presence of two molecules in the asymmetric unit, the calculated Matthews coefficient was 2.58 A(3) Da(-1), which corresponds to a solvent content of 52.3%. For MAD phasing, a four-wavelength data set was collected at 3.0 A resolution.

SUBMITTER: Kang GB

PROVIDER: S-EPMC2864684 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of MinE, the cell-division topological specificity factor from Helicobacter pylori.

Kang Gil Bu GB Song Hye Eun HE Kim Mun Kyoung MK Youn Hyung Seop HS An Jun Yop JY Lee Jung Gyu JG Park Kyung Ryung KR Eom Soo Hyun SH

Acta crystallographica. Section F, Structural biology and crystallization communications 20100429 Pt 5

Cell division in Gram-negative bacteria is driven by the formation of an FtsZ ring at the division site. MinE regulates the proper placement of the FtsZ ring at mid-cell by blocking the inhibitory action of the MinCD complex. Diffraction data were collected at 2.8 A resolution from a native crystal of full-length Helicobacter pylori MinE. The crystal belonged to space group P6(4). Assuming the presence of two molecules in the asymmetric unit, the calculated Matthews coefficient was 2.58 A(3) Da( ...[more]

PMID: 20445251

Similar Datasets

Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor.

Project description:In Gram-negative bacteria, proper placement of the FtsZ ring, mediated by nucleoid occlusion and the activities of the dynamic oscillating Min proteins MinC, MinD and MinE, is required for correct positioning of the cell division septum. MinE is a topological specificity factor that counters the activity of MinCD division inhibitor at the mid-cell division site. Its structure consists of an anti-MinCD domain and a topology specificity domain (TSD). Previous NMR analysis of truncated Escherichia coli MinE showed that the TSD domain contains a long alpha-helix and two anti-parallel beta-strands, which mediate formation of a homodimeric alpha/beta structure. Here we report the crystal structure of full-length Helicobacter pylori MinE and redefine its TSD based on that structure. The N-terminal region of the TSD (residues 19-26), previously defined as part of the anti-MinCD domain, forms a beta-strand (betaA) and participates in TSD folding. In addition, H. pylori MinE forms a dimer through the interaction of anti-parallel betaA-strands. Moreover, we observed serial dimer-dimer interactions within the crystal packing, resulting in the formation of a multimeric structure. We therefore redefine the functional domain of MinE and propose that a multimeric filamentous structure is formed through anti-parallel beta-strand interactions.

| S-EPMC2883074 | biostudies-literature

Crystallization and preliminary crystallographic studies of Helicobacter pylori arginase.

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Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp6.

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Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase.

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Expression, purification, crystallization and preliminary X-ray analysis of an NAD-dependent glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori.

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Expression, purification, crystallization and preliminary X-ray analysis of an NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori.

Project description:The classical glycolytic pathway contains an NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, with NADP-dependent forms reserved for photosynthetic organisms and archaea. Here, the cloning, expression, purification, crystallization and preliminary X-ray analysis of an NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori is reported; crystals of the protein were grown both in the presence and the absence of NADP.

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