1dhp
From Proteopedia
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| - | [[Image:1dhp.gif|left|200px]] | + | [[Image:1dhp.gif|left|200px]] |
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| - | '''DIHYDRODIPICOLINATE SYNTHASE''' | + | {{Structure |
| + | |PDB= 1dhp |SIZE=350|CAPTION= <scene name='initialview01'>1dhp</scene>, resolution 2.3Å | ||
| + | |SITE= <scene name='pdbsite=S1:Pyruvate+Binding+Residue'>S1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] | ||
| + | |GENE= DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''DIHYDRODIPICOLINATE SYNTHASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DHP is a [ | + | 1DHP 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=1DHP OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution., Mirwaldt C, Korndorfer I, Huber R, J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:[http:// | + | The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution., Mirwaldt C, Korndorfer I, Huber R, J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7853400 7853400] |
[[Category: Dihydrodipicolinate synthase]] | [[Category: Dihydrodipicolinate synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: synthase]] | [[Category: synthase]] | ||
| - | ''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 10:38:41 2008'' |
Revision as of 08:38, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Gene: | DAPA (Escherichia coli) | ||||||
| Activity: | Dihydrodipicolinate synthase, with EC number 4.2.1.52 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIHYDRODIPICOLINATE SYNTHASE
Overview
The crystal structure of dihydrodipicolinate synthase from E. coli was determined by multiple isomorphous replacement methods. The structure was refined at a resolution of 2.5 A and the final R-factor is 19.6% for 32,190 reflections between 10.0 A and 2.5 A and F > 2 sigma (F). The crystallographic asymmetric unit contains two monomers related by approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is built up by crystallographic symmetry. The tetramer is almost planar with no contacts between the subunits related by the non-crystallographic dyad. The active sites are accessible from a wide water-filled channel in the center of the tetramer. The dihydrodipicolinate synthase monomer is composed of two domains. Each polypeptide chain is folded into an 8-fold alpha/beta barrel and a C-terminal alpha-helical domain comprising residues 224 to 292. The fold is similar to that of N-acetylneuraminate lyase. The active site lysine 161 is located in the alpha/beta barrel and has access via two entrances from the C-terminal side of the barrel.
About this Structure
1DHP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution., Mirwaldt C, Korndorfer I, Huber R, J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:7853400
Page seeded by OCA on Thu Mar 20 10:38:41 2008
