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| {{STRUCTURE_1g8t| PDB=1g8t | SCENE= }} | | {{STRUCTURE_1g8t| PDB=1g8t | SCENE= }} |
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| '''SM ENDONUCLEASE FROM SERATIA MARCENSCENS AT 1.1 A RESOLUTION'''
| | ===SM ENDONUCLEASE FROM SERATIA MARCENSCENS AT 1.1 A RESOLUTION=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10771425}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10771425 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10771425}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nuclease]] | | [[Category: Nuclease]] |
| [[Category: Signal]] | | [[Category: Signal]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:17:19 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:53:57 2008'' |
