1P5V	Chaperone, Structural Protein	date	Apr 28, 2003
title	X-Ray Structure Of The Caf1m:Caf1 Chaperone:Subunit Preassembly Complex
authors	A.V.Zavialov, J.Berglund, A.F.Pudney, L.J.Fooks, T.M.Ibrahim, S.Macintyre, S.D.Knight
compound		source
Molecule: Chaperone Protein Caf1m Chain: A Fragment: Residues 24-258 Of Sws P26926 Synonym: Caf1m Chaperone; Caf1m; Capsule Protein Fraction 1; F1 Chaperone Protein; Engineered: Yes		Organism_scientific: Yersinia Pestis Organism_common: Bacteria Strain: Kim5 Gene: Caf1m Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_variant: B834 (De3) Expression_system_vector_type: Plasmid Expression_system_plasmid: Pfm-1-6h
Molecule: F1 Capsule Antigen Chain: B Fragment: Residues 35-170 Of Sws P26948 Engineered: Yes Other_details: His-Tagged Fragment Of F1 Capsule		Organism_scientific: Yersinia Pestis Organism_common: Bacteria Strain: Kim5 Gene: Caf1 Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_variant: B834 (De3) Expression_system_vector_type: Plasmid Expression_system_plasmid: Pfm-1-6h
symmetry	Space Group: P 1 21 1	R_factor	0.198
crystal cell	length a length b length c angle alpha angle beta angle gamma 36.000 69.230 69.110 90.00 92.96 90.00
method	X-Ray Diffraction	resolution	1.70 Å
note	1P5V is a representative structure
similarity	Belongs to the periplasmic pilus chaperone family. Contains 1 ig-like (immunoglobulin-like) domain.[Pili_assembly_N]
subcellular loc.	Periplasmic. Capsule.
genes	caf1, caf1M, pMT082, pMT084, y1098, y1100, y5194, y5196 (Y. pestis)
function	It seems to interact with the subunit polypeptide and to prevent it from digestion by a protease. Has a stimulatory role for the envelope antigen f1 secretion.
Gene Ontology	Chain Function Process Component A protein binding unfolded protein binding protein folding cell wall organization and b... outer membrane-bounded perip... periplasmic space B
Primary reference	Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation., Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, MacIntyre S, Knight SD, Cell 2003 May 30;113(5):587-96. PMID:12787500

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (69 Kb) [Save to disk] Biological Unit Coordinates (1p5v.pdb1.gz) 55 Kb CSU: Contacts of Structural Units for 1P5V Likely Quarternary Molecular Structure file(s) for 1P5V Retrieve 1P5V in mmCIF format [Save to disk]

View 1P5V in 3D

On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure. On FirstGlance, an excellent tool for a guided tour on the structure components, by E. Martz. On AstexViewer, from MSD-EBI (viewer documentation). On RasMol (Install RasMol freeware) Here's help on how to use RasMol.

Visual 3D analysis of 1P5V

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Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1P5V, from MSDmotif at EBI Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1p5va2, region A:148-233 [Jmol] [rasmolscript] [script source]     - Domain d1p5va1, region A:7-147 [Jmol] [rasmolscript] [script source]     - Domain d1p5vb_, region B [Jmol] [rasmolscript] [script source] Fold representative 1p5v from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1p5v_B] [1p5v_A]

Other resources with information on 1P5V

InterPro: IPR001829 MMDB (Entrez's Structure Database)

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