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4BYZ

Structural characterization using Sulfur-SAD of the cytoplasmic domain of Burkholderia pseudomallei PilO2Bp, an actin-like protein component of a Type IVb R64-derivative pilus machinery.

Summary for 4BYZ
Entry DOI10.2210/pdb4byz/pdb
Related4BZ0
DescriptorTYPE IV PILUS BIOSYNTHESIS PROTEIN, PHOSPHATE ION, POTASSIUM ION, ... (4 entities in total)
Functional Keywordsmotor protein
Biological sourceBURKHOLDERIA PSEUDOMALLEI
Total number of polymer chains1
Total formula weight22489.71
Authors
Lassaux, P.,Manjasetty, B.A.,Conchillo-Sole, O.,Yero, D.,Gourlay, L.,Perletti, L.,Daura, X.,Belrhali, H.,Bolognesi, M. (deposition date: 2013-07-22, release date: 2014-04-23, Last modification date: 2024-05-08)
Primary citationLassaux, P.,Conchillo-Sole, O.,Manjasetty, B.A.,Yero, D.,Perletti, L.,Belrhali, H.,Daura, X.,Gourlay, L.J.,Bolognesi, M.
Redefining the Pf06864 Pfam Family Based on Burkholderia Pseudomallei Pilo2BP S-Sad Crystal Structure.
Plos One, 9:94981-, 2014
Cited by
PubMed Abstract: Type IV pili are surface-exposed filaments and bacterial virulence factors, represented by the Tfpa and Tfpb types, which assemble via specific machineries. The Tfpb group is further divided into seven variants, linked to heterogeneity in the assembly machineries. Here we focus on PilO2(Bp), a protein component of the Tfpb R64 thin pilus variant assembly machinery from the pathogen Burkholderia pseudomallei. PilO2(Bp) belongs to the PF06864 Pfam family, for which an improved definition is presented based on newly derived Hidden Markov Model (HMM) profiles. The 3D structure of the N-terminal domain of PilO2(Bp) (N-PilO2(Bp)), here reported, is the first structural representative of the PF06864 family. N-PilO2(Bp) presents an actin-like ATPase fold that is shown to be present in BfpC, a different variant assembly protein; the new HMM profiles classify BfpC as a PF06864 member. Our results provide structural insight into the PF06864 family and on the Type IV pili assembly machinery.
PubMed: 24728008
DOI: 10.1371/JOURNAL.PONE.0094981
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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