Structural highlights
Function
[Q5SLM3_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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
