3hq2
BsuCP Crystal StructureBsuCP Crystal Structure
Structural highlights
Function[CBP1_BACSU] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. Has lower activity with substrates ending with His or Trp.[1] 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 PubMedM32 carboxypeptidases are a distinct family of HEXXH metalloproteases whose structures exhibit a narrow substrate groove that is blocked at one end. Structural alignments with other HEXXH metalloprotease-peptide complexes suggested an orientation in which the substrate is directed towards the back of the groove. This led us to hypothesize, and subsequently confirm that the maximum substrate length for M32 carboxypeptidases is restricted. Structural and sequence analyses implicate a highly conserved Arg at the back of the groove as being critical for this length restriction. However, the Thermus thermophilus and Bacillus subtilis M32 members lack this conserved Arg. Herein, we present the biochemical and structural characterization of these two proteins. Our findings support the important role of the conserved Arg in maintaining the length restriction, and reveal a proline-rich loop as an alternate blocking strategy. Based on our results, we propose that M32 carboxypeptidases from Bacilli belong to a separate subfamily. Proteins 2009. (c) 2009 Wiley-Liss, Inc. Insight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies.,Lee MM, Isaza CE, White JD, Chen RP, Liang GF, He HT, Chan SI, Chan MK Proteins. 2009 May 11;77(3):647-657. PMID:19544567[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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