1dhp

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[[Image:1dhp.gif|left|200px]]
[[Image:1dhp.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1dhp |SIZE=350|CAPTION= <scene name='initialview01'>1dhp</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1dhp", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=S1:Pyruvate+Binding+Residue'>S1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1dhp| PDB=1dhp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB]</span>
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}}
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'''DIHYDRODIPICOLINATE SYNTHASE'''
'''DIHYDRODIPICOLINATE SYNTHASE'''
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[[Category: Korndoerfer, I.]]
[[Category: Korndoerfer, I.]]
[[Category: Mirwaldt, C.]]
[[Category: Mirwaldt, C.]]
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[[Category: dihydrodipicolinate]]
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[[Category: Dihydrodipicolinate]]
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[[Category: synthase]]
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[[Category: Synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:51:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:41:45 2008''
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Revision as of 10:51, 2 May 2008

Image:1dhp.gif

Template:STRUCTURE 1dhp

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 Fri May 2 13:51:31 2008

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