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3V16

An intramolecular pi-cation latch in phosphatidylinositol-specific phospholipase C from S.aureus controls substrate access to the active site

Summary for 3V16
Entry DOI10.2210/pdb3v16/pdb
Descriptor1-phosphatidylinositol phosphodiesterase, 1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE, CHLORIDE ION, ... (4 entities in total)
Functional Keywordspi-cation, tim barrel, phospholipase, lyase
Biological sourceStaphylococcus aureus subsp. aureus
Total number of polymer chains1
Total formula weight34499.77
Authors
Goldstein, R.I.,Cheng, J.,Stec, B.,Roberts, M.F. (deposition date: 2011-12-09, release date: 2012-04-04, Last modification date: 2023-09-13)
Primary citationGoldstein, R.,Cheng, J.,Stec, B.,Roberts, M.F.
Structure of the S. aureus PI-Specific Phospholipase C Reveals Modulation of Active Site Access by a Titratable PI-Cation Latched Loop
Biochemistry, 51:2579-2587, 2012
Cited by
PubMed: 22390775
DOI: 10.1021/bi300057q
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

217705

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