2PRQ

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica

Summary for 2PRQ

• Entry DOI: 10.2210/pdb2prq/pdb
• Related: 1AMP 1LOK
• Descriptor: Bacterial leucyl aminopeptidase, COBALT (II) ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: tris, peptidase, aminohydrolase, cobalt, metalloprotease, hydrolase
• Biological source: Vibrio proteolyticus
• Cellular location: Secreted : Q01693
• Total number of polymer chains: 1
• Total formula weight: 31667.36

Authors

Munih, P.,Moulin, A.,Stamper, C.C.,Bennet, B.,Ringe, D.,Petsko, G.A.,Holz, R.C. (deposition date: 2007-05-04, release date: 2007-06-12, Last modification date: 2024-11-13)

Primary citation

Munih, P.,Moulin, A.,Stamper, C.C.,Bennett, B.,Ringe, D.,Petsko, G.A.,Holz, R.C.
X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica.
J.Inorg.Biochem., 101:1099-1107, 2007

PubMed Abstract: The X-ray crystal structure of the Co(II)-loaded form of the aminopeptidase from Aeromonas proteolytica ([CoCo(AAP)]) was solved to 2.2A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandwiched between alpha-helices, identical to [ZnZn(AAP)]. Co(II) binding to AAP does not introduce any major conformational changes to the overall protein structure and the amino acid residues ligated to the dicobalt(II) cluster in [CoCo(AAP)] are the same as those in the native Zn(II)-loaded structure with only minor perturbations in bond lengths. The Co(II)-Co(II) distance is 3.3A. Tris(hydroxymethyl)aminomethane (Tris) coordinates to the dinuclear Co(II) active site of AAP with one of the Tris hydroxyl oxygen atoms (O4) forming a single oxygen atom bridge between the two Co(II) ions. This is the only Tris atom coordinated to the metals with Co1-O and Co2-O bonds distances of 2.2 and 1.9A, respectively. Each of the Co(II) ions resides in a distorted trigonal bipyramidal geometry. This important structure bridges the gap between previous structural and spectroscopic studies performed on AAP and is discussed in this context.

PubMed: 17574677
DOI: 10.1016/j.jinorgbio.2007.03.010

Experimental method

X-RAY DIFFRACTION (2.15 Å)