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1ql0
From Proteopedia
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'''SM ENDONUCLEASE FROM SERATIA MARCENSCENS AT ATOMIC RESOLUTION''' | '''SM ENDONUCLEASE FROM SERATIA MARCENSCENS AT ATOMIC RESOLUTION''' | ||
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[[Category: Mikhailov, A M.]] | [[Category: Mikhailov, A M.]] | ||
[[Category: Perbandt, M.]] | [[Category: Perbandt, M.]] | ||
| - | [[Category: | + | [[Category: Endonuclease]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Magnesium]] |
| - | [[Category: | + | [[Category: Nuclease]] |
| - | [[Category: | + | [[Category: Signal]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:24:05 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:24, 3 May 2008
SM ENDONUCLEASE FROM SERATIA MARCENSCENS AT ATOMIC RESOLUTION
Overview
The three-dimensional crystal structure of Serratia marcescens endonuclease has been refined at 1.1 A resolution to an R factor of 12.9% and an R(free) of 15.6% with the use of anisotropic temperature factors. The model contains 3694 non-H atoms, 715 water molecules, four sulfate ions and two Mg(2+)-binding sites at the active sites of the homodimeric protein. It is shown that the magnesium ion linked to the active-site Asn119 of each monomer is surrounded by five water molecules and shows an octahedral coordination geometry. The temperature factors for the bound Mg(2+) ions in the A and B subunits are 7.08 and 4.60 A(2), respectively, and the average temperature factors for the surrounding water molecules are 12.13 and 10.3 A(2), respectively. In comparison with earlier structures, alternative side-chain conformations are defined for 51 residues of the dimer, including the essential active-site residue Arg57. A plausible mechanism of enzyme function is proposed based on the high-resolution S. marcescens nuclease structure, the functional characteristics of the natural and mutational forms of the enzyme and consideration of its structural analogy with homing endo-nuclease I-PpoI.
About this Structure
1QL0 is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.
Reference
Atomic structure of the Serratia marcescens endonuclease at 1.1 A resolution and the enzyme reaction mechanism., Shlyapnikov SV, Lunin VV, Perbandt M, Polyakov KM, Lunin VY, Levdikov VM, Betzel C, Mikhailov AM, Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):567-72. PMID:10771425 Page seeded by OCA on Sat May 3 06:24:05 2008
