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Structure paper

TitleSubangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 128, Page 9086-9102, Year 2006
Publish dateMay 25, 2006 (structure data deposition date)
AuthorsFuhrmann, C.N. / Daugherty, M.D. / Agard, D.A.
External linksJ. Am. Chem. Soc. / PubMed:16834383
MethodsX-ray diffraction
Resolution0.82 - 0.9 Å
Structure data

PDB-2h5c:
0.82A resolution crystal structure of alpha-lytic protease at pH 5
Method: X-RAY DIFFRACTION / Resolution: 0.82 Å

PDB-2h5d:
0.9A resolution crystal structure of alpha-lytic protease complexed with a transition state analogue, MeOSuc-Ala-Ala-Pro-Val boronic acid
Method: X-RAY DIFFRACTION / Resolution: 0.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • lysobacter enzymogenes (bacteria)
KeywordsHYDROLASE / A-LYTIC PROTEASE / SERINE PROTEASE / ACYLATION TRANSITION STATE / CATALYSIS / PROTEIN FOLDING / PROTEIN STABILITY / PACKING DISTORTION / HYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR COMPLEX

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