3PY5

Crystal structure of a beta-lactamase-like protein from brucella melitensis bound to AMP

Summary for 3PY5

• Entry DOI: 10.2210/pdb3py5/pdb
• Related: 3md7
• Descriptor: Beta-lactamase-like, MANGANESE (II) ION, POTASSIUM ION, ... (6 entities in total)
• Functional Keywords: ssgcid, beta-lactamase like, brucella melitensis, gmp, amp, mn centre, structural genomics, seattle structural genomics center for infectious disease, hydrolase
• Biological source: Brucella melitensis biovar Abortus
• Total number of polymer chains: 1
• Total formula weight: 31372.02

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-12-11, release date: 2010-12-29, Last modification date: 2023-09-13)

Primary citation

Abendroth, J.,Sankaran, B.,Edwards, T.E.,Gardberg, A.S.,Dieterich, S.,Bhandari, J.,Napuli, A.J.,Van Voorhis, W.C.,Staker, B.L.,Myler, P.J.,Stewart, L.J.
BrabA.11339.a: anomalous diffraction and ligand binding guide towards the elucidation of the function of a `putative beta-lactamase-like protein from Brucella melitensis.
Acta Crystallogr.,Sect.F, 67:1106-1112, 2011

PubMed Abstract: The crystal structure of a β-lactamase-like protein from Brucella melitensis was initially solved by SAD phasing from an in-house data set collected on a crystal soaked with iodide. A high-resolution data set was collected at a synchroton at the Se edge wavelength, which also provided an independent source of phasing using a small anomalous signal from metal ions in the active site. Comparisons of anomalous peak heights at various wavelengths allowed the identification of the active-site metal ions as manganese. In the native data set a partially occupied GMP could be identified. When co-crystallized with AMPPNP or GMPPNP, clear density for the hydrolyzed analogs was observed, providing hints to the function of the protein.

PubMed: 21904058
DOI: 10.1107/S1744309111010220

Experimental method

X-RAY DIFFRACTION (1.7 Å)