› 1hqb

Solution NMR

TERTIARY STRUCTURE OF APO-D-ALANYL CARRIER PROTEIN

Released:
DOI: 10.2210/pdb1hqb/pdb
PDB entry 1hqb coloured by chain, front view.
PDB entry 1hqb coloured by chain, side view.
PDB entry 1hqb coloured by chain, top view.
Source organism: Lacticaseibacillus casei
Primary publication:
Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein.
Volkman BF, Zhang Q, Debabov DV, Rivera E, Kresheck GC, Neuhaus FC
Biochemistry 40 7964-72 (2001)
PMID: 11434765

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169958 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanyl carrier protein Chain: A
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 8.8 KDa
Source organism: Lacticaseibacillus casei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03AZ0 (Residues: 2-81; Coverage: 99%)
Gene names: LSEI_0796, dltC
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

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Citations

10 review citations

The structural biology of type II fatty acid biosynthesis.
White et al. (2005)
9 more

3 mentions without citation

A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria.
Neuhaus et al. (2003)
2 more