1W74

X-ray structure of peptidyl-prolyl cis-trans isomerase A, PpiA, Rv0009, from Mycobacterium tuberculosis.

1W74 の概要

• エントリーDOI: 10.2210/pdb1w74/pdb
• 分子名称: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A (2 entities in total)
• 機能のキーワード: isomerase, peptidyl-prolyl cis-trans isomerase, cyclophilin, ppiase, rv0009, rotamase, structural proteomics in europe, spine, structural genomics
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• 細胞内の位置: Cytoplasm (By similarity): P71578
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40606.89

構造登録者

Henriksson, L.M.,Johansson, P.,Unge, T.,Mowbray, S.L. (登録日: 2004-08-27, 公開日: 2004-10-20, 最終更新日: 2023-12-13)

主引用文献

Henriksson, L.M.,Johansson, P.,Unge, T.,Mowbray, S.L.
X-Ray Structure of Peptidyl-Prolyl Cis-Trans Isomerase a from Mycobacterium Tuberculosis
Eur.J.Biochem., 271:4107-, 2004

PubMed Abstract: Peptidyl-prolyl cis-trans isomerases (EC 5.2.1.8) catalyse the interconversion of cis and trans peptide bonds and are therefore considered to be important for protein folding. They are also thought to participate in processes such as signalling, cell surface recognition, chaperoning and heat-shock response. Here we report the soluble expression of recombinant Mycobacterium tuberculosis peptidyl-prolyl cis-trans isomerase PpiA in Escherichia coli, together with an investigation of its structure and biochemical properties. The protein was shown to be active in a spectrophotometric assay, with an estimated kcat/Km of 2.0 x 10(6) m(-1).s(-1). The X-ray structure of PpiA was solved by molecular replacement, and refined to a resolution of 2.6 A with R and Rfree values of 21.3% and 22.9%, respectively. Comparisons to known structures show that the PpiA represents a slight variation on the peptidyl-prolyl cis-trans isomerase fold, previously not represented in the Protein Data Bank. Inspection of the active site suggests that specificity for substrates and cyclosporin A will be similar to that found for most other enzymes of this structural family. Comparison to the sequence of the second M. tuberculosis enzyme, PpiB, suggests that binding of peptide substrates as well as cyclosporin A may differ in that case.

PubMed: 15479239
DOI: 10.1111/J.1432-1033.2004.04348.X

実験手法

X-RAY DIFFRACTION (2.6 Å)