1qae

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|PDB= 1qae |SIZE=350|CAPTION= <scene name='initialview01'>1qae</scene>, resolution 2.05&Aring;
|PDB= 1qae |SIZE=350|CAPTION= <scene name='initialview01'>1qae</scene>, resolution 2.05&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Serratia_marcescens_nuclease Serratia marcescens nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.30.2 3.1.30.2]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Serratia_marcescens_nuclease Serratia marcescens nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.30.2 3.1.30.2] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qae OCA], [http://www.ebi.ac.uk/pdbsum/1qae PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qae RCSB]</span>
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[[Category: Krause, K L.]]
[[Category: Krause, K L.]]
[[Category: Miller, M D.]]
[[Category: Miller, M D.]]
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[[Category: MG]]
 
[[Category: dnase]]
[[Category: dnase]]
[[Category: magnesium]]
[[Category: magnesium]]
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[[Category: sugar-nonspecific nuclease]]
[[Category: sugar-nonspecific nuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:35:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:00 2008''

Revision as of 20:11, 30 March 2008


PDB ID 1qae

Drag the structure with the mouse to rotate
, resolution 2.05Å
Ligands:
Activity: Serratia marcescens nuclease, with EC number 3.1.30.2
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED MAGNESIUM-WATER CLUSTER


Overview

Serratia endonuclease is an important member of a class of magnesium dependent nucleases that are widely distributed in nature. Here, we describe the location and geometry of a magnesium-water cluster within the active site of this enzyme. The sole protein ligand of the magnesium atom is Asn119; this metal ion is also associated with five water molecules to complete an octahedral coordination complex. These water molecules are very well ordered and there is no evidence of rotational disorder or motion. Glu127 and His89 are located nearby and each is hydrogen bonded to water molecules in the coordination sphere. Asp86 is not chelated to the magnesium or its surrounding water molecules. Results of kinetics and site-specific mutagenesis experiments suggest that this metal-water cluster contains the catalytic metal ion of this enzyme. All residues which hydrogen bond to the water molecules that coordinate the magnesium atom are conserved in nucleases homologous to Serratia endonuclease, suggesting that the water cluster is a conserved feature of this family of enzymes. We offer a detailed structural comparison to one other nuclease, the homing endonuclease I-PpoI, that has recently been shown, in spite of a lack of sequence homology, to share a similar active site geometry to Serratia endonuclease. Evidence from both of these structures suggests that the magnesium of Serratia nuclease participates in catalysis via an inner sphere mechanism.

About this Structure

1QAE is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.

Reference

The active site of Serratia endonuclease contains a conserved magnesium-water cluster., Miller MD, Cai J, Krause KL, J Mol Biol. 1999 May 21;288(5):975-87. PMID:10329193

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