1dhp
From Proteopedia
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| - | [[Image:1dhp.gif|left|200px]]<br /> | + | [[Image:1dhp.gif|left|200px]]<br /><applet load="1dhp" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dhp" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1dhp, resolution 2.3Å" /> | caption="1dhp, resolution 2.3Å" /> | ||
'''DIHYDRODIPICOLINATE SYNTHASE'''<br /> | '''DIHYDRODIPICOLINATE SYNTHASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DHP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] | + | 1DHP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=S1:Pyruvate Binding Residue'>S1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: synthase]] | [[Category: synthase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:44:34 2007'' |
Revision as of 12:34, 18 December 2007
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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 with K as ligand. Active as Dihydrodipicolinate synthase, with EC number 4.2.1.52 Known structural/functional Site: . 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
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