1I1I

NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE

Summary for 1I1I

• Entry DOI: 10.2210/pdb1i1i/pdb
• Descriptor: NEUROLYSIN, ZINC ION (3 entities in total)
• Functional Keywords: neuropeptidase, zinc metallopeptidase, endopeptidase, hydrolase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Mitochondrion intermembrane space: P42676
• Total number of polymer chains: 1
• Total formula weight: 78005.68

Authors

Brown, C.K.,Madauss, K.,Lian, W.,Tolbert, W.D.,Beck, M.R.,Rodgers, D.W. (deposition date: 2001-02-01, release date: 2001-02-28, Last modification date: 2024-02-07)

Primary citation

Brown, C.K.,Madauss, K.,Lian, W.,Beck, M.R.,Tolbert, W.D.,Rodgers, D.W.
Structure of neurolysin reveals a deep channel that limits substrate access.
Proc.Natl.Acad.Sci.USA, 98:3127-3132, 2001

PubMed Abstract: 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.

PubMed: 11248043
DOI: 10.1073/pnas.051633198

Experimental method

X-RAY DIFFRACTION (2.3 Å)