<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gov ConSurf].
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Revision as of 20:44, 7 February 2016
RIBONUCLEASE BI(G SPECIFIC ENDONUCLEASE) COMPLEXED WITH SULFATE IONS
1gov is a 2 chain structure with sequence from Bacillus intermedius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 structures of Bacillus intermedius ribonuclease (binase), an extracellular 109-residue enzyme, and its complexes with 3'GMP and sulfate ions were solved at 1.65 and 2.0 A, respectively. The structures were refined using REFMAC. The crystal of free binase belongs to the space group C2, whereas the crystals of complexes belong to the space group P2(1)2(1)2(1). In both crystal lattices the asymmetric unit contains two molecules which form an identical dimer. The structure of the dimer is such that only one of its subunits can bind the nucleotide in the 3'GMP-binase complex, where the guanyl base is located in the recognition loop of the enzyme. In both binase complex structures the phosphate group of 3'GMP or one of the sulfate ions make an electrostatic interaction with the binase molecule at the catalytic site. A second phosphate-binding site was found in the structures of the complexes at the cleft formed by the loop 34-39, the main chain of Arg82 and the side chain of Trp34. Comparison of the complex and unliganded enzyme crystal structures shows that there are some small but distinct differences in the specificity loop (56-62) and in the loops 34-39 and 99-104 associated with the binding of the nucleotide and sulfate ions.
The structure of substrate-free microbial ribonuclease binase and of its complexes with 3'GMP and sulfate ions.,Polyakov KM, Lebedev AA, Okorokov AL, Panov KI, Schulga AA, Pavlovsky AG, Karpeisky MY, Dodson GG Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):744-50. Epub 2002, Apr 26. PMID:11976484[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Polyakov KM, Lebedev AA, Okorokov AL, Panov KI, Schulga AA, Pavlovsky AG, Karpeisky MY, Dodson GG. The structure of substrate-free microbial ribonuclease binase and of its complexes with 3'GMP and sulfate ions. Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):744-50. Epub 2002, Apr 26. PMID:11976484