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Structural determinants of SecB recognition by SecA in bacterial protein translocation

Structural determinants of SecB recognition by SecA in bacterial protein translocation

http://www.wikidata.org/entity/Q27642253

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SecA, a remarkable nanomachine Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA Structural basis for the antifolding activity of a molecular chaperone Zinc coordination is essential for the function and activity of the type II secretion ATPase EpsE Orientation of SecA and SecB in complex, derived from disulfide cross-linking Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE The structural view of bacterial translocation-specific chaperone SecB: implications for function.Multitasking SecB chaperones in bacteria SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis.The basis of asymmetry in the SecA:SecB complex.Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis.The bacterial Sec-translocase: structure and mechanism.Emerging themes in SecA2-mediated protein export.Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.SecYEG activates GTPases to drive the completion of cotranslational protein targeting.SecB--a chaperone dedicated to protein translocation.Breaking on through to the other side: protein export through the bacterial Sec system.The Canonical and Accessory Sec System of Gram-positive Bacteria.Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.Covalently dimerized SecA is functional in protein translocation.Penetration into Membrane of Amino-terminal Region of SecA when Associated with SecYEG in Active Complexes.The Sec System: Protein Export in Escherichia coli.

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

http://www.wikidata.org/entity/Q27642253

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2003 nî lūn-bûn

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2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2003 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Nature structural biology

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Structural determinants of SecB recognition by SecA in bacterial protein translocation

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Jiahai Zhou

http://www.w3.org/2001/XMLSchema#string

Zhaohui Xu

http://www.w3.org/2001/XMLSchema#string

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Processing of X-ray diffraction data collected in oscillation mode

Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum

Crystal structure of the bacterial protein export chaperone secB

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

Whole-genome random sequencing and assembly of Haemophilus influenzae Rd

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scholarly article

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10.1038/NSB980

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11

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10

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2003-11-01T00:00:00Z

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9072876

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1046463710

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