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| [[Image:1dhp.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1dhp| PDB=1dhp | SCENE= }} | | {{STRUCTURE_1dhp| PDB=1dhp | SCENE= }} |
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| '''DIHYDRODIPICOLINATE SYNTHASE'''
| | ===DIHYDRODIPICOLINATE SYNTHASE=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_7853400}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7853400 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7853400}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Dihydrodipicolinate]] | | [[Category: Dihydrodipicolinate]] |
| [[Category: Synthase]] | | [[Category: Synthase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:51:31 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:04:54 2008'' |
