3ZYP

Cellulose induced protein, Cip1

Summary for 3ZYP

• Entry DOI: 10.2210/pdb3zyp/pdb
• Descriptor: CIP1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: metal binding protein, calcium-binding, cbm-containing, beta sandwich jelly roll, carbohydrate-binding
• Biological source: HYPOCREA JECORINA
• Total number of polymer chains: 1
• Total formula weight: 24436.78

Authors

Jacobson, F.,Karkehabadi, S.,Hansson, H.,Goedegebuur, F.,Wallace, L.,Mitchinson, C.,Piens, K.,Stals, I.,Sandgren, M. (deposition date: 2011-08-24, release date: 2012-09-12, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)