3md7 | pdb_00003md7

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

spinqualitylabelsall models 3md7, resolution 1.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3md7 is a 1 chain structure with sequence from Brucella abortus 2308. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.27Å Ligands: 5GP, K, MN, NA, TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2YQ74_BRUA2 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 The crystal structure of a beta-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. 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.,Abendroth J, Sankaran B, Edwards TE, Gardberg AS, Dieterich S, Bhandari J, Napuli AJ, Van Voorhis WC, Staker BL, Myler PJ, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1106-12. Epub 2011 Aug 16. PMID:21904058 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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