› 1le8

X-ray diffraction
2.3Å resolution

Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex

Released:
DOI: 10.2210/pdb1le8/pdb
PDB entry 1le8 coloured by chain, front view.
PDB entry 1le8 coloured by chain, side view.
PDB entry 1le8 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural and thermodynamic characterization of the DNA binding properties of a triple alanine mutant of MATalpha2.
Ke A, Mathias JR, Vershon AK, Wolberger C
Structure 10 961-71 (2002)
PMID: 12121651

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-114132 (preferred)
Entry contents:
2 distinct polypeptide molecules
2 distinct DNA molecules
Macromolecules (4 distinct):
Mating-type protein A1 Chain: A
Molecule details ›
Chain: A
Length: 53 amino acids
Theoretical weight: 6.28 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P0CY10 (Residues: 74-126; Coverage: 42%)
Gene names: MAT1A, MATA1
Sequence domains: Homeodomain
Structure domains: Homeodomain-like
Mating-type protein ALPHA2 Chain: B
Molecule details ›
Chain: B
Length: 83 amino acids
Theoretical weight: 9.63 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CY08 (Residues: 128-210; Coverage: 40%)
Gene names: ALPHA-2, MAT2A, MATAL2, MATALPHA2, YCR039C, YCR39C
Sequence domains: Homeodomain
Structure domains: Homeodomain-like
5'-D(*AP*CP*AP*TP*GP*TP*AP*AP*AP*AP*AP*TP*TP*TP*AP*CP*AP*TP*CP*A)-3' Chain: C
Molecule details ›
Chain: C
Length: 20 nucleotides
Theoretical weight: 6.11 KDa
5'-D(*TP*TP*GP*AP*TP*GP*TP*AP*AP*AP*TP*TP*TP*TP*TP*AP*CP*AP*TP*G)-3' Chain: D
Molecule details ›
Chain: D
Length: 20 nucleotides
Theoretical weight: 6.15 KDa

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P65
Unit cell:
a: 54.17Å b: 54.17Å c: 164.23Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.256 0.256 0.299
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

A survey of the year 2002 literature on applications of isothermal titration calorimetry.
Cliff et al. (2003)
5 other articles

9 mentions without citation

Assessment of helical interfaces in protein-protein interactions.
Jochim et al. (2009)
8 more