User:Yongmin Kim

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== Yongmin Kim, Kwangse Lee, Siwoo Kim ==
== Yongmin Kim, Kwangse Lee, Siwoo Kim ==
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== '''Assignment #1''' ==
 
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'''Exercise I'''
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== '''Glutamic Amino Acid Binding Site''' ==
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'''Backbone representation in Rainbow Color'''
 
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<scene name='Glu_Binding_Site/Rainbow/5'>Backbone Trace with Ligand</scene>
 
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Glutamate is the first substrate to bind glutamate synthetase.
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'''Exercise II'''
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'''Ligand and Chain selection with Labeling'''
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<scene name='Glu_Binding_Site/Rainbow2/1'>Labeled Ligands in Chain A</scene>
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'''Exercise III'''
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'''Active Site Residues'''
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<scene name='User:Yongmin_Kim/Exercise_3/1'>Active Site Residues</scene>
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== '''Assignment#2''' ==
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'''Glutamic Amino Acid Binding Site'''
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Glutamic amino acid is a product of the hydrolysis of proteins, and it is created by Glutamine in Proteins. It means that glutamine is converted to Glutamic amino acid during the hydrolysis of proteins. In Glutamine Synthetase, Glutamic amino acid binds well with Nitrogen of ATP.
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The interaction of main-chain carbonyl oxygen containing Nitrogen in Glutamine Synthetase, is replaced by one with the side-chain of Glu-325 and Ser-154.[http://www.ncbi.nlm.nih.gov/pubmed/10708854] The amino acid residues Ser-53 and Asn-264 stabilize Glutamic acid in the binding site.
The interaction of main-chain carbonyl oxygen containing Nitrogen in Glutamine Synthetase, is replaced by one with the side-chain of Glu-325 and Ser-154.[http://www.ncbi.nlm.nih.gov/pubmed/10708854] The amino acid residues Ser-53 and Asn-264 stabilize Glutamic acid in the binding site.

Revision as of 05:09, 16 December 2008

We, Yongmin Kim, Kwangse Lee, and Siwoo Kim, are biology major students at University of Maryland Baltimore Counry, We are enrolled in BIO430 (BioChem), we are planning to complete a project on an aspect of the structure and function of prokaryote glutamine synthetase.


BioChem Practice

Drag the structure with the mouse to rotate

Yongmin Kim, Kwangse Lee, Siwoo Kim

Glutamic Amino Acid Binding Site

Glutamate is the first substrate to bind glutamate synthetase.

The interaction of main-chain carbonyl oxygen containing Nitrogen in Glutamine Synthetase, is replaced by one with the side-chain of Glu-325 and Ser-154.[1] The amino acid residues Ser-53 and Asn-264 stabilize Glutamic acid in the binding site.

Phosphinothricin resides with glutamate substrate pocket and stabilizes the Glu-327 flap in a site which hinders the access of glutamate into the active site, by holding the inhibitor in the enzyme.[2]

When Glutamic amino acid binds in inhibitor Phosphinothricin between Glu-324 ~ 329, only Glu-327 flap which appears when MetSox or Phosphinothricin binds to Glutamine Synthatase will stabilize the orientation of phosphinyl group by guard the glutamate entrance into the bifunnel.[3]


Reference

[1] Krajewski, W. W., et.al.,Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights, Proc Natl Acad Sci 2005, 102; 10499-10504.

[2] Gill, H & Eisenberg, D., Biochemistry 2001 40: 1903-1912

[3] Eisenberg, D., et.al., Structure-function relationships of glutamine synthetases, Biochim Biophys Acta 2000: 1477, 122-145.

Proteopedia Page Contributors and Editors (what is this?)

Yongmin Kim, Eran Hodis

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