1lni
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(New page: 200px<br /><applet load="1lni" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lni, resolution 1.0Å" /> '''CRYSTAL STRUCTURE ANA...)
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Revision as of 18:34, 20 November 2007
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CRYSTAL STRUCTURE ANALYSIS OF A RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS AT ATOMIC RESOLUTION (1.0 A)
Overview
Ribonuclease from Streptomyces aureofaciens, the bacterial source for the, industrial production of chlorotetracycline, is a guanylate, endoribonuclease (RNase Sa; EC 3.1.27.3) which hydrolyses the, phosphodiester bonds of single-stranded RNA at the 3'-side of guanosine, nucleotides with high specificity. The structure of the enzyme was, previously refined at atomic resolution (1.2 A) using room-temperature, data. Here, the RNase Sa structure refined against 1.0 A data collected at, cryogenic temperature is reported. There are two surface loops in molecule, A and one in molecule B for which two main-chain conformations are, modelled: these loops contain active-site residues. The separation for, most of the corresponding main-chain atoms in the two conformations is, about 0.8 A, with a maximum of 2.5 A. The two regions of dual conformation, represent the most important differences in comparison with the structure, determined at room temperature, where the corresponding loops have one, conformation only but the largest degree of anisotropy. The flexibility of, the loops observed in the structure of RNase Sa is directly linked to the, need for the active site to interact productively with substrates and/or, inhibitors.
About this Structure
1LNI is a Single protein structure of sequence from Streptomyces aureofaciens with SO4 and GOL as ligands. Active as Ribonuclease T(1), with EC number 3.1.27.3 Full crystallographic information is available from OCA.
Reference
Atomic resolution data reveal flexibility in the structure of RNase Sa., Sevcik J, Lamzin VS, Dauter Z, Wilson KS, Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1307-13. Epub 2002, Jul 20. PMID:12136142
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