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1JQ6

HUMAN CYTOMEGALOVIRUS PROTEASE DIMER-INTERFACE MUTANT, S225Y

Summary for 1JQ6
Entry DOI10.2210/pdb1jq6/pdb
Related1JQ7 1WPO 2WPO
DescriptorASSEMBLIN (2 entities in total)
Functional Keywordsherpesvirus, cytomegalovirus, serine protease, dimerization, enzyme activity regulation, hydrolase
Biological sourceHuman herpesvirus 5 (Human cytomegalovirus)
Cellular locationProtease precursor: Host cytoplasm. Assemblin: Host nucleus. Assembly protein: Host nucleus: P16753
Total number of polymer chains1
Total formula weight28518.59
Authors
Batra, R.,Khayat, R.,Tong, L. (deposition date: 2001-08-03, release date: 2001-09-12, Last modification date: 2024-10-30)
Primary citationBatra, R.,Khayat, R.,Tong, L.
Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease.
Nat.Struct.Biol., 8:810-817, 2001
Cited by
PubMed Abstract: Biochemical studies indicate that dimerization is required for the catalytic activity of herpesvirus proteases, whereas structural studies show a complete active site in each monomer, away from the dimer interface. Here we report kinetic, biophysical and crystallographic characterizations of structure-based mutants in the dimer interface of human cytomegalovirus (HCMV) protease. Such mutations can produce a 1,700-fold reduction in the kcat while having minimal effects on the K(m). Dimer stability is not affected by these mutations, suggesting that dimerization itself is insufficient for activity. There are large changes in monomer conformation and dimer organization of the apo S225Y mutant enzyme. However, binding of an activated peptidomimetic inhibitor induced a conformation remarkably similar to the wild type protease. Our studies suggest that appropriate dimer formation may be required to indirectly stabilize the protease oxyanion hole, revealing a novel mechanism for dimerization to regulate enzyme activity.
PubMed: 11524687
DOI: 10.1038/nsb0901-810
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

239149

數據於2025-07-23公開中

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