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[[ | ==Crystal structure of a beta-lactamase-like protein from brucella melitensis bound to AMP== | ||
<StructureSection load='3py5' size='340' side='right' caption='[[3py5]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3py5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brucella_abortus Brucella abortus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PY5 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3md7|3md7]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAB1_1016 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=235 Brucella abortus])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3py5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3py5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3py5 RCSB], [http://www.ebi.ac.uk/pdbsum/3py5 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:21904058</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Brucella abortus]] | [[Category: Brucella abortus]] | ||
[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]] | [[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]] | ||
Revision as of 08:33, 4 June 2014
Crystal structure of a beta-lactamase-like protein from brucella melitensis bound to AMPCrystal structure of a beta-lactamase-like protein from brucella melitensis bound to AMP
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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