1ka4 | pdb_00001ka4
Structure of Pyrococcus furiosus carboxypeptidase Nat-Pb
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| 1ka4, resolution 3.00Å | |||||||||||||
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| Ligands: | PB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1KA4 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus., Arndt JW, Hao B, Ramakrishnan V, Cheng T, Chan SI, Chan MK, Structure. 2002 Feb;10(2):215-24. PMID:11839307
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