1i1i
From Proteopedia
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| , resolution 2.3Å | |||||||
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| Ligands: | |||||||
| Activity: | Neurolysin, with EC number 3.4.24.16 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE
Overview
The zinc metallopeptidase neurolysin is shown by x-ray crystallography to have large structural elements erected over the active site region that allow substrate access only through a deep narrow channel. This architecture accounts for specialization of this neuropeptidase to small bioactive peptide substrates without bulky secondary and tertiary structures. In addition, modeling studies indicate that the length of a substrate N-terminal to the site of hydrolysis is restricted to approximately 10 residues by the limited size of the active site cavity. Some structural elements of neurolysin, including a five-stranded beta-sheet and the two active site helices, are conserved with other metallopeptidases. The connecting loop regions of these elements, however, are much extended in neurolysin, and they, together with other open coil elements, line the active site cavity. These potentially flexible elements may account for the ability of the enzyme to cleave a variety of sequences.
About this Structure
1I1I is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of neurolysin reveals a deep channel that limits substrate access., Brown CK, Madauss K, Lian W, Beck MR, Tolbert WD, Rodgers DW, Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3127-32. Epub 2001 Mar 6. PMID:11248043
Page seeded by OCA on Thu Mar 20 11:44:20 2008
