Structural highlights
Function
[CBP1_THET8] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro. Has lower activity with substrates ending with Gly or Glu.[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 PubMed
Carboxypeptidase 1 from the thermophilic eubacterium Thermus thermophilus (TthCP1, 58 kDa), a member of the M32 family of metallocarboxypeptidases, was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals diffracted X-rays to beyond 2.6 A resolution using a synchrotron-radiation source. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 171.0, b = 231.6, c = 124.9 A. The crystal contains three molecules in an asymmetric unit (VM = 2.11 A3 Da(-1)) and has a solvent content of 61.5%.
Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus.,Nagata K, Tsutsui S, Lee WC, Ito K, Kamo M, Inoue Y, Tanokura M Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1445-6. Epub 2004, Jul 21. PMID:15272172[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee MM, Isaza CE, White JD, Chen RP, Liang GF, He HT, Chan SI, Chan MK. Insight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies. Proteins. 2009 May 11;77(3):647-657. PMID:19544567 doi:10.1002/prot.22478
- ↑ Nagata K, Tsutsui S, Lee WC, Ito K, Kamo M, Inoue Y, Tanokura M. Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus. Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1445-6. Epub 2004, Jul 21. PMID:15272172 doi:10.1107/S0907444904012557
