ISDA: 1CCI

Deposition Date 1996-12-18

Release Date 1997-07-07

Last Version Date 2026-08-12

Entry Detail

PDB ID:

1CCI

Keywords:

OXIDOREDUCTASE

Title:

HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP

Biological Source:

Source Organism(s):

Saccharomyces cerevisiae (Taxon ID: 4932)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.40 Å

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:CYTOCHROME C PEROXIDASE
Gene (Uniprot):CCP1
Mutagens:INS(MKT) AT N-TERMINUS, T53I, D152G, F202
Chain IDs:A
Chain Length:294
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae

UniProt ID:P00431 Pfam ID:PF00141 EC:1.11.1.5

Ligand Molecules

DMI

HEM

Primary Citation

A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity.

Fitzgerald, M.M, Musah, R.A, McRee, D.E, Goodin, D.B.Show

Nat.Struct.Biol. 3 626 631 (1996)

PMID: 8673607 DOI: 10.1038/nsb0796-626

Abstact

Conformational changes that gate the access of substrates or ligands to an active site are important features of enzyme function. In this report, we describe an unusual example of a structural rearrangement near a buried artificial cavity in cytochrome c peroxidase that occurs on binding protonated benzimidazole. A hinged main-chain rotation at two residues (Pro 190 and Asn 195) results in a surface loop rearrangement that opens a large solvent-accessible channel for the entry of ligands to an otherwise inaccessible binding site. The trapping of this alternate conformational state provides a unique view of the extent to which protein dynamics can allow small molecule penetration into buried protein cavities.

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Primary Citation of related structures

Abstact

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