Wild type TrCel7A catalytic domain in a closed stateWild type TrCel7A catalytic domain in a closed state

Structural highlights

5tc9 is a 1 chain structure with sequence from Trichoderma reesei QM6a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G0RVK1_HYPJQ

Publication Abstract from PubMed

Trichoderma reesei Cel7A efficiently hydrolyses cellulose. We report here the crystallographic structures of the wild-type TrCel7A catalytic domain (CD) in an open state and, for the first time, in a closed state. Molecular dynamics (MD) simulations indicate that the loops along the CD tunnel move in concerted motions. Together, the crystallographic and MD data suggest that the CD cycles between the tense and relaxed forms that are characteristic of work producing enzymes. Analysis of the interactions formed by R251 provides a structural rationale for the concurrent decrease in product inhibition and catalytic efficiency measured for product-binding site mutants.

Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states.,Bodenheimer AM, Meilleur F FEBS Lett. 2016 Dec;590(23):4429-4438. doi: 10.1002/1873-3468.12464. Epub 2016, Nov 7. PMID:27943301[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Bodenheimer AM, Meilleur F. Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states. FEBS Lett. 2016 Dec;590(23):4429-4438. doi: 10.1002/1873-3468.12464. Epub 2016, Nov 7. PMID:27943301 doi:http://dx.doi.org/10.1002/1873-3468.12464

5tc9, resolution 1.60Å

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