3ZYP

Cellulose induced protein, Cip1

3ZYP の概要

• エントリーDOI: 10.2210/pdb3zyp/pdb
• 分子名称: CIP1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: metal binding protein, calcium-binding, cbm-containing, beta sandwich jelly roll, carbohydrate-binding
• 由来する生物種: HYPOCREA JECORINA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24436.78

構造登録者

Jacobson, F.,Karkehabadi, S.,Hansson, H.,Goedegebuur, F.,Wallace, L.,Mitchinson, C.,Piens, K.,Stals, I.,Sandgren, M. (登録日: 2011-08-24, 公開日: 2012-09-12, 最終更新日: 2024-10-16)

主引用文献

Jacobson, F.,Karkehabadi, S.,Hansson, H.,Goedegebuur, F.,Wallace, L.,Mitchinson, C.,Piens, K.,Stals, I.,Sandgren, M.
The Crystal Structure of the Core Domain of a Cellulose Induced Protein (Cip1) from Hypocrea Jecorina, at 1.5 A Resolution.
Plos One, 8:70562-, 2013

PubMed Abstract: In an effort to characterise the whole transcriptome of the fungus Hypocrea jecorina, cDNA clones of this fungus were identified that encode for previously unknown proteins that are likely to function in biomass degradation. One of these newly identified proteins, found to be co-regulated with the major H. jecorina cellulases, is a protein that was denoted Cellulose induced protein 1 (Cip1). This protein consists of a glycoside hydrolase family 1 carbohydrate binding module connected via a linker region to a domain with yet unknown function. After cloning and expression of Cip1 in H. jecorina, the protein was purified and biochemically characterised with the aim of determining a potential enzymatic activity for the novel protein. No hydrolytic activity against any of the tested plant cell wall components was found. The proteolytic core domain of Cip1 was then crystallised, and the three-dimensional structure of this was determined to 1.5 Å resolution utilising sulphur single-wavelength anomalous dispersion phasing (sulphor-SAD). A calcium ion binding site was identified in a sequence conserved region of Cip1 and is also seen in other proteins with the same general fold as Cip1, such as many carbohydrate binding modules. The presence of this ion was found to have a structural role. The Cip1 structure was analysed and a structural homology search was performed to identify structurally related proteins. The two published structures with highest overall structural similarity to Cip1 found were two poly-lyases: CsGL, a glucuronan lyase from H. jecorina and vAL-1, an alginate lyase from the Chlorella virus. This indicates that Cip1 may be a lyase. However, initial trials did not detect significant lyase activity for Cip1. Cip1 is the first structure to be solved of the 23 currently known Cip1 sequential homologs (with a sequence identity cut-off of 25%), including both bacterial and fungal members.

PubMed: 24039705
DOI: 10.1371/JOURNAL.PONE.0070562

実験手法

X-RAY DIFFRACTION (1.5 Å)