2BZR

Crystal structure of accD5 (Rv3280), an acyl-CoA carboxylase beta- subunit from Mycobacterium tuberculosis

PDB DOI: https://doi.org/10.2210/pdb2BZR/pdb

Classification: TRANSFERASE
Organism(s): Mycobacterium tuberculosis H37Rv
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2005-08-22 Released: 2007-01-02
Deposition Author(s): Holton, S.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.211
R-Value Work: 0.176
R-Value Observed: 0.178

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Structural Diversity in the Six-Fold Redundant Set of Acyl-Coa Carboxyltransferases in Mycobacterium Tuberculosis.

Holton, S.J., King-Scott, S., Eddine, A.N., Kaufmann, S.H., Wilmanns, M.

(2006) FEBS Lett 580: 6898

PubMed: 17157300 Search on PubMed
DOI: https://doi.org/10.1016/j.febslet.2006.11.054
Primary Citation of Related Structures:
2BZR

PubMed Abstract:
Mycobacterium tuberculosis contains multiple versions of the accA and accD genes that encode the alpha- and beta-subunits of at least three distinct multi-functional acyl-CoA carboxylase complexes. Because of its proposed involvement in pathogenic M. tuberculosis survival, the high-resolution crystal structure of the beta-subunit gene accD5 product has been determined and reveals a hexameric 356 kDa complex. Analysis of the active site properties of AccD5 and homology models of the other five M. tuberculosis AccD homologues reveals unexpected differences in their surface composition, providing a molecular rational key for a sorting mechanism governing correct acyl-CoA carboxylase holo complex assembly in M. tuberculosis.

Organizational Affiliation

EMBL c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.

Macromolecule Content

Total Structure Weight: 356.17 kDa
Atom Count: 24,961
Modelled Residue Count: 3,041
Deposited Residue Count: 3,288
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
PROPIONYL-COA CARBOXYLASE BETA CHAIN 5	A, B, C, D, E A, B, C, D, E, F	548	Mycobacterium tuberculosis H37Rv	Mutation(s): 0 EC: 6.4.1.3
UniProt
Find proteins for P9WQH7 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)) Explore P9WQH7 Go to UniProtKB: P9WQH7
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P9WQH7
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.211
R-Value Work: 0.176
R-Value Observed: 0.178
Space Group: P 4₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 173.562	α = 90
b = 173.562	β = 90
c = 339.823	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
TRUNCATE	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2007-01-02

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2007-01-02
Type: Initial release
Version 1.1: 2011-05-08
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.