1K9X

Structure of Pyrococcus furiosus carboxypeptidase Apo-Yb

Summary for 1K9X

• Entry DOI: 10.2210/pdb1k9x/pdb
• Related: 1KA2 1KA4
• Descriptor: M32 carboxypeptidase (2 entities in total)
• Functional Keywords: hexxh motif, m32 family, metallopeptidase, carboxypeptidase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 4
• Total formula weight: 236510.66

Authors

Arndt, J.W.,Hao, B.,Ramakrishnan, V.,Cheng, T.,Chan, S.I.,Chan, M.K. (deposition date: 2001-10-31, release date: 2002-11-06, Last modification date: 2024-02-07)

Primary citation

Arndt, J.W.,Hao, B.,Ramakrishnan, V.,Cheng, T.,Chan, S.I.,Chan, M.K.
Crystal Structure of a Novel Carboxypeptidase from the Hyperthermophilic Archaeon Pyrococcus furiosus
Structure, 10:215-224, 2002

PubMed Abstract: The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly, the structure is similar to the recently reported rat neurolysin. Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues. The roles for these conserved residues in the catalytic mechanism are inferred based on modeling and their location.

PubMed: 11839307
DOI: 10.1016/S0969-2126(02)00698-6

Experimental method

X-RAY DIFFRACTION (2.3 Å)