1v4a
From Proteopedia
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| - | [[Image:1v4a.jpg|left|200px]] | + | [[Image:1v4a.jpg|left|200px]] |
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| - | '''Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase''' | + | {{Structure |
| + | |PDB= 1v4a |SIZE=350|CAPTION= <scene name='initialview01'>1v4a</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/[Glutamate--ammonia-ligase]_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.42 2.7.7.42] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V4A is a [ | + | 1V4A 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=1V4A OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase., Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL, Structure. 2004 May;12(5):861-9. PMID:[http:// | + | Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase., Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL, Structure. 2004 May;12(5):861-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15130478 15130478] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: main alpha helix]] | [[Category: main alpha helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:40:38 2008'' |
Revision as of 12:40, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Activity: | [Glutamate--ammonia-ligase_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number 2.7.7.42 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase
Overview
We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase beta, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polbeta-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding.
About this Structure
1V4A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase., Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL, Structure. 2004 May;12(5):861-9. PMID:15130478[[Category: [Glutamate--ammonia-ligase] adenylyltransferase]]
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