1l9w
From Proteopedia
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| - | [[Image:1l9w. | + | [[Image:1l9w.jpg|left|200px]]<br /><applet load="1l9w" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1l9w" size=" | + | |
caption="1l9w, resolution 2.10Å" /> | caption="1l9w, resolution 2.10Å" /> | ||
'''CRYSTAL STRUCTURE OF 3-DEHYDROQUINASE FROM SALMONELLA TYPHI COMPLEXED WITH REACTION PRODUCT'''<br /> | '''CRYSTAL STRUCTURE OF 3-DEHYDROQUINASE FROM SALMONELLA TYPHI COMPLEXED WITH REACTION PRODUCT'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L9W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhi Salmonella typhi] with DHS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] Full crystallographic information is available from [http:// | + | 1L9W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhi Salmonella typhi] with <scene name='pdbligand=DHS:'>DHS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:17:16 2008'' |
Revision as of 14:17, 15 February 2008
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CRYSTAL STRUCTURE OF 3-DEHYDROQUINASE FROM SALMONELLA TYPHI COMPLEXED WITH REACTION PRODUCT
Overview
The type I 3-dehydroquinate dehydratase (DHQase) which catalyses the, reversible dehydration of 3-dehydroquinic acid to 3-dehydroshikimic acid, is involved in the shikimate pathway for the biosynthesis of aromatic, compounds. The shikimate pathway is absent in mammals, which makes, structural information about DHQase vital for the rational design of, antimicrobial drugs and herbicides. The crystallographic structure of the, type I DHQase from Salmonella typhi has now been determined for the native, form at 1.78 A resolution (R = 19.9%; R(free) = 24.7%). The structure of, the modified enzyme to which the product has been covalently bound has, also been determined but in a different crystal form (2.1 A resolution; R, = 17.7%; R(free) = 24.5%). An analysis of the three available crystal, forms has provided information about the physiological dimer interface., The enzyme relies upon the closure of a lid-like loop to complete its, active site. As the lid-loop tends to stay in the closed position, dimerization appears to play a role in biasing the arrangement of the loop, towards its open position, thus facilitating substrate access.
About this Structure
1L9W is a Single protein structure of sequence from Salmonella typhi with as ligand. Active as 3-dehydroquinate dehydratase, with EC number 4.2.1.10 Full crystallographic information is available from OCA.
Reference
Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity., Lee WH, Perles LA, Nagem RA, Shrive AK, Hawkins A, Sawyer L, Polikarpov I, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):798-804. Epub 2002, Apr 26. PMID:11976491
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