2x8j

Intracellular subtilisin precursor from B. clausii

spinqualitylabelsall models 2x8j, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x8j is a 6 chain structure with sequence from Atcc 700160. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, GOL, NA NonStd Res: CSX Related: 2wv7, 2wwt Activity: Subtilisin, with EC number 3.4.21.62 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 The intracellular subtilisin proteases (ISPs) are the only known members of the important and ubiquitous subtilisin family that function exclusively within the cell, constituting a major component of the degradome in many Gram-positive bacteria. The first ISP structure reported herein at a spacing of 1.56 A reveals features unique among subtilisins that has enabled potential functional and physiological roles to be assigned to sequence elements exclusive to the ISPs. Unlike all other subtilisins, ISP from B. clausii is dimeric, with residues from the C terminus making a major contribution to the dimer interface by crossing over to contact the partner subunit. A short N-terminal extension binds back across the active site to provide a potential novel regulatory mechanism of intrinsic proteolytic activity: a proline residue conserved throughout the ISPs introduces a kink in the polypeptide backbone that lifts the target peptide bond out of reach of the catalytic residues. Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.,Vevodova J, Gamble M, Kunze G, Ariza A, Dodson E, Jones DD, Wilson KS Structure. 2010 Jun 9;18(6):744-55. PMID:20541512 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Subtilisin

Proteopedia Page Contributors and Editors (what is this?)

OCA