1KA4

Structure of Pyrococcus furiosus carboxypeptidase Nat-Pb

1KA4 の概要

• エントリーDOI: 10.2210/pdb1ka4/pdb
• 関連するPDBエントリー: 1k9x 1ka2
• 分子名称: M32 carboxypeptidase, LEAD (II) ION (3 entities in total)
• 機能のキーワード: hexxh motif, m32 family, metallopeptidase, carboxypeptidase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59334.86

構造登録者

Arndt, J.W.,Hao, B.,Ramakrishnan, V.,Cheng, T.,Chan, S.I.,Chan, M.K. (登録日: 2001-10-31, 公開日: 2002-11-06, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3 Å)