1goc: Difference between revisions

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[[Image:1goc.gif|left|200px]]<br /><applet load="1goc" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1goc.gif|left|200px]]
caption="1goc, resolution 2.0&Aring;" />
 
'''COOPERATIVE STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY INSERTION OF GLY-80B AND GLY-77-> ALA SUBSTITUTION'''<br />
{{Structure
|PDB= 1goc |SIZE=350|CAPTION= <scene name='initialview01'>1goc</scene>, resolution 2.0&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4]
|GENE=
}}
 
'''COOPERATIVE STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY INSERTION OF GLY-80B AND GLY-77-> ALA SUBSTITUTION'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1GOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOC OCA].  
1GOC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOC OCA].  


==Reference==
==Reference==
Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77--&gt;Ala substitution., Ishikawa K, Nakamura H, Morikawa K, Kimura S, Kanaya S, Biochemistry. 1993 Jul 20;32(28):7136-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8393706 8393706]
Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77--&gt;Ala substitution., Ishikawa K, Nakamura H, Morikawa K, Kimura S, Kanaya S, Biochemistry. 1993 Jul 20;32(28):7136-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8393706 8393706]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Ribonuclease H]]
[[Category: Ribonuclease H]]
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[[Category: hydrolase(endoribonuclease)]]
[[Category: hydrolase(endoribonuclease)]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:17 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:25:48 2008''

Revision as of 12:25, 20 March 2008

File:1goc.gif


PDB ID 1goc

Drag the structure with the mouse to rotate
, resolution 2.0Å
Activity: Ribonuclease H, with EC number 3.1.26.4
Coordinates: save as pdb, mmCIF, xml



COOPERATIVE STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY INSERTION OF GLY-80B AND GLY-77-> ALA SUBSTITUTION


OverviewOverview

The insertion of a Gly residue (designated as Gly-80b) between the C-cap of the alpha II-helix (Gln-80) and the N-cap of the alpha III-helix (Trp-81) in Escherichia coli ribonuclease HI enhances the protein stability by 0.4 kcal/mol in delta G (Kimura, S., Nakamura, H., Hashimoto, T., Oobatake, M., & Kanaya, S. (1992) J. Biol. Chem. 267, 21535-21542). Another mutation within the alpha II-helix, Gly-77-->Ala, reduces the stability by 0.9 kcal/mol. Simultaneous introduction of these mutations enhances the stability by 0.8 kcal/mol, indicating that the effects of these mutations are cooperative and not simply independent. We determined the crystal structures of these three mutant proteins (G80b-, A77-, and A77/G80b-RNase H) to investigate this cooperative mechanism of the protein stabilization. The structures revealed that the inserted Gly-80b assumes a left-handed helical conformation in both the G80b- and the A77/G80b-RNase H. This inserted glycine residue allows the formation of a "paperclip", which is a common motif at the C-termini of alpha-helices. Accompanying the formation of the paperclip motif, two intrahelical hydrogen bonds are formed between the backbone atoms (O78-N80b and O80b-N84). The stabilization caused by the insertion of Gly-80b can be ascribed to the formation of these hydrogen bonds. The Gly-77-->Ala substitution destabilizes the protein due to the deformed packing interactions in the hydrophobic core around Ala-77 and the stress in the wedged indole ring of Trp-81. These effects are alleviated by the insertion of Gly-80b, which relaxes the backbone structure.(ABSTRACT TRUNCATED AT 250 WORDS)

About this StructureAbout this Structure

1GOC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution., Ishikawa K, Nakamura H, Morikawa K, Kimura S, Kanaya S, Biochemistry. 1993 Jul 20;32(28):7136-42. PMID:8393706

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