1uc9
From Proteopedia
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|PDB= 1uc9 |SIZE=350|CAPTION= <scene name='initialview01'>1uc9</scene>, resolution 2.38Å | |PDB= 1uc9 |SIZE=350|CAPTION= <scene name='initialview01'>1uc9</scene>, resolution 2.38Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1uc8|1UC8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uc9 OCA], [http://www.ebi.ac.uk/pdbsum/1uc9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uc9 RCSB]</span> | ||
}} | }} | ||
| Line 33: | Line 36: | ||
[[Category: Vassylyeva, M N.]] | [[Category: Vassylyeva, M N.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: ADP]] | ||
[[Category: alpha-aminoadipate pathway]] | [[Category: alpha-aminoadipate pathway]] | ||
[[Category: lysine biosynthesis]] | [[Category: lysine biosynthesis]] | ||
| Line 40: | Line 42: | ||
[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:08:18 2008'' |
Revision as of 21:08, 30 March 2008
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| , resolution 2.38Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1UC8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8
Overview
The thermophilic bacterium Thermus thermophilus synthesizes lysine through the alpha-aminoadipate pathway, which uses alpha-aminoadipate as a biosynthetic intermediate of lysine. LysX is the essential enzyme in this pathway, and is believed to catalyze the acylation of alpha-aminoadipate. We have determined the crystal structures of LysX and its complex with ADP at 2.0A and 2.38A resolutions, respectively. LysX is composed of three alpha+beta domains, each composed of a four to five-stranded beta-sheet core flanked by alpha-helices. The C-terminal and central domains form an ATP-grasp fold, which is responsible for ATP binding. LysX has two flexible loop regions, which are expected to play an important role in substrate binding and protection. In spite of the low level of sequence identity, the overall fold of LysX is surprisingly similar to that of other ATP-grasp fold proteins, such as D-Ala:D-Ala ligase, PurT-encoded glycinamide ribonucleotide transformylase, glutathione synthetase, and synapsin I. In particular, they share a similar spatial arrangement of the amino acid residues around the ATP-binding site. This observation strongly suggests that LysX is an ATP-utilizing enzyme that shares a common evolutionary ancestor with other ATP-grasp fold proteins possessing a carboxylate-amine/thiol ligase activity.
About this Structure
1UC9 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8., Sakai H, Vassylyeva MN, Matsuura T, Sekine S, Gotoh K, Nishiyama M, Terada T, Shirouzu M, Kuramitsu S, Vassylyev DG, Yokoyama S, J Mol Biol. 2003 Sep 19;332(3):729-40. PMID:12963379
Page seeded by OCA on Mon Mar 31 00:08:18 2008
Categories: Single protein | Thermus thermophilus | Kuramitsu, S. | Matsuura, T. | Nishiyama, M. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sakai, H. | Sekine, S. | Shirouzu, M. | Terada, T. | Vassylyev, D G. | Vassylyeva, M N. | Yokoyama, S. | Alpha-aminoadipate pathway | Lysine biosynthesis | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
