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The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica.
High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei.
Three high-resolution crystal structures of different catalytically deficient mutants of CBHI in complex with cellotetraose, cellopentaose and cellohexaose have been refined and support the hypothesis that hydrolysis by CBHI proceeds from the reducing towards the non-reducing end of a cellulose chain, and they provide a structural explanation for the observed distribution of initial Hydrolysis products.
Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance…
The solution structure of a synthetic 36-residue polypeptide comprising the C-terminal cellulose binding domain of cellobiohydrolase I (CT-CBH I) from Trichoderma reesei was investigated by nuclear…
The Uppsala Electron-Density Server.
- G. Kleywegt, M. Harris, J. Zou, T. C. Taylor, A. Wählby, T. Jones
- PhysicsActa Crystallographica Section D: Biological…
- 1 December 2004
An account is provided of the methods that are used to generate the information contained in the Uppsala Electron Density Server and some of the problems that are encountered in the map-generation process.
Crystal Structures of a Poplar Xyloglucan Endotransglycosylase Reveal Details of Transglycosylation Acceptor Binding
The structure of XET in complex with a xyloglucan nonasaccharide, XLLG, reveals a very favorable acceptor binding site, which is a necessary but not sufficient prerequisite for transglycosylation.
Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols.
A structural explanation for the high stereoselectivity of CALB toward many secondary alcohols is provided and the tetrahedral intermediates of two chiral substrates have been modeled on the basis of available structural and biochemical information.
Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG.
Protein G and protein A have developed different strategies for binding to Fc, whereas the protein G:Fc complex involves mainly charged and polar contacts, whereas protein A and Fc are held together through non-specific hydrophobic interactions and a few polar interactions.
The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
A possible binding site for retinol in BLG has been identified by model-building and a role for BLG in vitamin A transport is suggested and specific receptors for the BLG–retinol complex in the intestine of neonate calves are discovered.
Lipid-binding proteins: a family of fatty acid and retinoid transport proteins.