1smn

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{{STRUCTURE_1smn| PDB=1smn | SCENE= }}
{{STRUCTURE_1smn| PDB=1smn | SCENE= }}
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'''IDENTIFICATION OF THE SERRATIA ENDONUCLEASE DIMER: STRUCTURAL BASIS AND IMPLICATIONS FOR CATALYSIS'''
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===IDENTIFICATION OF THE SERRATIA ENDONUCLEASE DIMER: STRUCTURAL BASIS AND IMPLICATIONS FOR CATALYSIS===
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==Overview==
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The Serratia endonuclease is an extracellularly secreted enzyme capable of cleaving both single- and double-stranded forms of DNA and RNA. It is the first member of a large class of related and usually dimeric endonucleases for which a structure is known. Using X-ray crystallography, the structure of monomer of this enzyme was reported by us previously (Miller MD et al., 1994, Nature Struct Biol 1:461-468). We now confirm the dimeric nature of this enzyme through light-scattering experiments and identify the physiologic dimer interface through crystal packing analysis. This dimerization occurs through an isologous twofold interaction localized to the carboxy-terminal subdomain of the enzyme. The dimer is a prolate ellipsoid with dimensions 30 A x 35 A x 90 A. The dimer interface is flat and contains four salt links, several hydrogen bonds, and nonpolar interactions. Buried water is prominent in this interface and it includes an unusual "cubic" water cluster. The position of the two active sites in the dimer suggests that they can act independently in their cleavage of DNA, but have a geometrical advantage in attacking substrate relative to the monomer.
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(as it appears on PubMed at http://www.pubmed.gov), where 8771193 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8771193}}
==About this Structure==
==About this Structure==
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[[Category: Rnase]]
[[Category: Rnase]]
[[Category: Sugar-nonspecific nuclease]]
[[Category: Sugar-nonspecific nuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:53:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:30:55 2008''

Revision as of 05:30, 29 July 2008

Image:1smn.png

Template:STRUCTURE 1smn

IDENTIFICATION OF THE SERRATIA ENDONUCLEASE DIMER: STRUCTURAL BASIS AND IMPLICATIONS FOR CATALYSIS

Template:ABSTRACT PUBMED 8771193

About this Structure

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

Reference

Identification of the Serratia endonuclease dimer: structural basis and implications for catalysis., Miller MD, Krause KL, Protein Sci. 1996 Jan;5(1):24-33. PMID:8771193

Page seeded by OCA on Tue Jul 29 08:30:55 2008

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