2vs2 | pdb_00002vs2

Neutron diffraction structure of endothiapepsin in complex with a gem- diol inhibitor.

spinqualitylabelsall models 2vs2, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vs2 is a 1 chain structure with sequence from Cryphonectria parasitica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 0QS, DOD NonStd Res: SUI Related: 1gvw, 5er1, 1ent, 4er4, 3er5, 1er8, 1epn, 1e81, 1e80, 5er2, 2er7, 1od1, 1gkt, 1epo, 1eed, 1gvv, 1oex, 2er0, 1oew, 2er9, 1epp, 4ape, 2v00, 1gvt, 1epl, 1epm, 4er1, 4er2, 1e82, 1gvx, 2jji, 2er6, 1e5o, 1gvu, 2jjj, 3er3, 1epr, 1epq Activity: Endothiapepsin, with EC number 3.4.23.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Hydrogen atoms play key roles in enzyme mechanism, but as this study shows, even high-quality X-ray data to a resolution of 1 A cannot directly visualize them. Neutron diffraction, however, can locate deuterium atoms even at resolutions around 2 A. Both neutron and X-ray diffraction data have been used to investigate the transition state of the aspartic proteinase endothiapepsin. The different techniques reveal a different part of the story, revealing the clearest picture yet of the catalytic mechanism by which the enzyme operates. Room temperature neutron and X-ray diffraction data were used in a newly developed joint refinement software package to visualize deuterium atoms within the active site of the enzyme when a gem-diol transition state analogue inhibitor is bound at the active site. These data were also used to estimate their individual occupancy, while analysis of the differences between the bond lengths of the catalytic aspartates was performed using atomic resolution X-ray data. The two methods are in agreement on the protonation state of the active site with a transition state analogue inhibitor bound confirming the catalytic mechanism at which the enzyme operates. The catalytic mechanism of an aspartic proteinase explored with neutron and X-ray diffraction.,Coates L, Tuan HF, Tomanicek S, Kovalevsky A, Mustyakimov M, Erskine P, Cooper J J Am Chem Soc. 2008 Jun 11;130(23):7235-7. Epub 2008 May 15. PMID:18479128 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin

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