3GLJ

A polymorph of carboxypeptidase B zymogen structure

3GLJ の概要

• エントリーDOI: 10.2210/pdb3glj/pdb
• 関連するPDBエントリー: 1NSA
• 分子名称: Carboxypeptidase B, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: procarboxypeptidase b cpb zymogen metalloprotease polymorphic form, carboxypeptidase, disulfide bond, hydrolase, metal-binding, metalloprotease, protease, secreted, zymogen
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted : P09955
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46410.95

構造登録者

Fernandez, D. (登録日: 2009-03-12, 公開日: 2009-10-20, 最終更新日: 2024-10-16)

主引用文献

Fernandez, D.,Boix, E.,Pallares, I.,Aviles, F.X.,Vendrell, J.
Analysis of a new crystal form of procarboxypeptidase B: further insights into the catalytic mechanism
Biopolymers, 2009

PubMed Abstract: A new triclinic crystal structure form of porcine pancreatic procarboxypeptidase B (PCPB) was obtained at higher resolution than the previously known tetragonal crystal structure. This new crystal polymorph has allowed for a corrected, accurate assignment of residues along the polypeptide chain based on the currently available gene sequence information and crystallographic data. The present structure shows unbound PCPB in a distinct molecular packing as compared to the previous benzamidine complexed form. Its catalytically important Tyr248 residue is oriented and hydrogen-bonded to solvent water molecules, and locates the furthest away from the catalytic zinc ion as compared to previous structures. A relatively long stretch of residues flanking Tyr248 and guarding the access to the catalytic zinc ion was found to be sequentially unique to the M14 family of peptidases. Predictions from a normal mode analysis indicated that this stretch of residues belongs to a rigid subdomain in the protein structure. The specific presence of a tyrosyl residue at the most exposed position in this region would allow for a delicate balance between extreme hydrophobicity and hydrophilicity, and affect substrate binding and the kinetic efficiency of the enzyme.

PubMed: 19802820
DOI: 10.1002/bip.21320

実験手法

X-RAY DIFFRACTION (1.89 Å)