2glt
From Proteopedia
(New page: 200px<br /><applet load="2glt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2glt, resolution 2.2Å" /> '''STRUCTURE OF ESCHERIC...) |
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| - | [[Image:2glt.gif|left|200px]]<br /><applet load="2glt" size=" | + | [[Image:2glt.gif|left|200px]]<br /><applet load="2glt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2glt, resolution 2.2Å" /> | caption="2glt, resolution 2.2Å" /> | ||
'''STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.'''<br /> | '''STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Escherichia coli B glutathione synthetase | + | The crystal structure of Escherichia coli B glutathione synthetase (GSHase) has been determined at the optimal catalytic condition pH 7.5. The most significant structural difference from the structure at pH 6.0 is the movement of the central domain towards the N-terminal domain almost as a rigid body. As a result of this movement, new interdomain and intersubunit polar interactions are formed which stabilize the dimeric structure further. The structure of GSHase at optimal pH was compared with 294 other known protein structures in terms of the spatial arrangements of secondary structural elements. Three enzymes (D-alanine: D-alanine ligase, succinyl-CoA synthetase and the biotin carboxylase subunit of acetyl-CoA carboxylase) were found to have structures similar to the ATP-binding site of GSHase, which extends across two domains. The ATP-binding sites in these four enzymes are composed of two antiparallel beta-sheets and are different from the classic mononucleotide-binding fold. Except for these proteins, no significant structural similarity was detected between GSHase and the other ATP-binding proteins. A structural motif in the N-terminal domain of GSHase has been found to be similar to the NAD-binding fold. This structural motif is shared by a number of other proteins that bind various negatively charged molecules. |
==About this Structure== | ==About this Structure== | ||
| - | 2GLT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure | + | 2GLT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1GLT. Active as [http://en.wikipedia.org/wiki/Glutathione_synthase Glutathione synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.3 6.3.2.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glutathione biosynthesis ligase]] | [[Category: glutathione biosynthesis ligase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:59 2008'' |
Revision as of 15:33, 21 February 2008
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STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.
Overview
The crystal structure of Escherichia coli B glutathione synthetase (GSHase) has been determined at the optimal catalytic condition pH 7.5. The most significant structural difference from the structure at pH 6.0 is the movement of the central domain towards the N-terminal domain almost as a rigid body. As a result of this movement, new interdomain and intersubunit polar interactions are formed which stabilize the dimeric structure further. The structure of GSHase at optimal pH was compared with 294 other known protein structures in terms of the spatial arrangements of secondary structural elements. Three enzymes (D-alanine: D-alanine ligase, succinyl-CoA synthetase and the biotin carboxylase subunit of acetyl-CoA carboxylase) were found to have structures similar to the ATP-binding site of GSHase, which extends across two domains. The ATP-binding sites in these four enzymes are composed of two antiparallel beta-sheets and are different from the classic mononucleotide-binding fold. Except for these proteins, no significant structural similarity was detected between GSHase and the other ATP-binding proteins. A structural motif in the N-terminal domain of GSHase has been found to be similar to the NAD-binding fold. This structural motif is shared by a number of other proteins that bind various negatively charged molecules.
About this Structure
2GLT is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1GLT. Active as Glutathione synthase, with EC number 6.3.2.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins., Matsuda K, Mizuguchi K, Nishioka T, Kato H, Go N, Oda J, Protein Eng. 1996 Dec;9(12):1083-92. PMID:9010922
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