PDBsum entry 1awr

Complex (isomerase/peptide)

PDB id: 1awr

Contents

Protein chains

(+ 0 more) 164 a.a. *

Ligands

HIS-ALA-GLY-PRO-ILE-ALA ×6

Waters ×175

* Residue conservation analysis

PDB id:

1awr

Name:

Complex (isomerase/peptide)

Title:

Cypa complexed with hagpia

Structure:

Cyclophilin a. Chain: a, b, c, d, e, f. Engineered: yes. Peptide from the HIV-1 capsid protein. Chain: g, h, i, j, k, l. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytoplasm. Gene: cyclophilin. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.58Å R-factor: 0.394 R-free: 0.461

Authors:

F.F.Vajdos

Key ref:

F.F.Vajdos et al. (1997). Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. Protein Sci, 6, 2297-2307. PubMed id: 9385632 DOI: 10.1002/pro.5560061103

Date:

04-Oct-97 Release date: 18-Mar-98

Protein chains

P62937  (PPIA_HUMAN) -  Peptidyl-prolyl cis-trans isomerase A from Homo sapiens

Seq: 165 a.a.

Struc: 164 a.a.

Enzyme reactions

• Enzyme class: E.C.5.2.1.8 - peptidylprolyl isomerase.
• Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1002/pro.5560061103

Protein Sci 6:2297-2307 (1997)

PubMed id: 9385632

Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.

F.F.Vajdos, S.Yoo, M.Houseweart, W.I.Sundquist, C.P.Hill.

ABSTRACT

The cellular protein, cyclophilin A (CypA), is incorporated into the virion of the type 1 human immunodeficiency virus (HIV-1) via a direct interaction with the capsid domain of the viral Gag polyprotein. We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex. In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. We also report the crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. Comparison with the recently determined structures of CypA in complexes with larger fragments of the HIV-1 capsid protein demonstrates that CypA recognition of these hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences.

Selected figure(s)

Figure 6.
Fig. 6. A: HAGPIA and CypA are shown in CPK and ribbon representa- tions, respectively. B: Orthogonal view. C: The molecular surface of CypA is colored gray and green according to curvature. CypA residues that in- teract with HAGPIA are shown, and residues that hydrogen bond (magen- ta) HAGPIA re in yellow. H drogen bonds are defined as acceptor to donor distances of less than 3.3 x. The HAGPIA N-terminal histidine and C-terminal alanine are labeled in For clarity, the side chains f the histidine and isoleucine have been omitted. Two ordered water that form bridging hydrogen bonds between peptide main chain and CypA active site residues are shown as blue spheres.

Figure 7.
Fig. 7. Superposition of HAGPIA and peptides refined in the pseudo (P4~)-cell. CypA CA atoms (residues 2-165) were overlapped by least squares (Kabsch, 976). CypA residues that hydrogen bond pep- tide ligands are HAGPIA (magenta), (cyan). Ala/Val 88 and the peptide proline residues are labeled.

The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (1997, 6, 2297-2307) copyright 1997.

Figures were selected by an automated process.