6B00

Thermostabilized mutant of human carbonic anhydrase II - A65T L100H K154N L224S L240P A248T

6B00 の概要

• エントリーDOI: 10.2210/pdb6b00/pdb
• 分子名称: Carbonic anhydrase 2, GLYCEROL, ZINC ION, ... (4 entities in total)
• 機能のキーワード: carbon sequestration, thermostable, protein engineering, lyase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm : P00918
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30287.28

構造登録者

Kean, K.M.,Karplus, P.A. (登録日: 2017-09-13, 公開日: 2017-12-13, 最終更新日: 2023-10-04)

主引用文献

Kean, K.M.,Porter, J.J.,Mehl, R.A.,Karplus, P.A.
Structural insights into a thermostable variant of human carbonic anhydrase II.
Protein Sci., 27:573-577, 2018

PubMed Abstract: Carbonic anhydrase is an enzyme of interest for many biotechnological developments including carbon sequestration. These applications often require harsh conditions, so there is a need for the development of thermostable variants. One of the most thermostable human carbonic anhydrase II (HCAIIts) variants was patented in 2006. Here, we report the ultra-high resolution crystal structure of HCAIIts. The structural changes seen are consistent with each of the six mutations involved acting largely independently and variously resulting in increased H-bonding, improved packing, and reduced side chain entropy loss on folding to yield the increased stability. We further suggest that for four of the mutations, improvements in backbone conformational energetics is also a contributor and that considerations of such conformational propensities of individual amino acids are often overlooked.

PubMed: 29139171
DOI: 10.1002/pro.3347

実験手法

X-RAY DIFFRACTION (0.9 Å)