1l9w

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[[Image:1l9w.jpg|left|200px]]<br /><applet load="1l9w" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l9w.jpg|left|200px]]
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caption="1l9w, resolution 2.10&Aring;" />
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'''CRYSTAL STRUCTURE OF 3-DEHYDROQUINASE FROM SALMONELLA TYPHI COMPLEXED WITH REACTION PRODUCT'''<br />
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{{Structure
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|PDB= 1l9w |SIZE=350|CAPTION= <scene name='initialview01'>1l9w</scene>, resolution 2.10&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=DHS:3-AMINO-4,5-DIHYDROXY-CYCLOHEX-1-ENECARBOXYLATE'>DHS</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF 3-DEHYDROQUINASE FROM SALMONELLA TYPHI COMPLEXED WITH REACTION PRODUCT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1L9W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhi Salmonella typhi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9W OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11976491 11976491]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11976491 11976491]
[[Category: 3-dehydroquinate dehydratase]]
[[Category: 3-dehydroquinate dehydratase]]
[[Category: Salmonella typhi]]
[[Category: Salmonella typhi]]
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[[Category: tim-barrel]]
[[Category: tim-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:23 2008''

Revision as of 10:28, 20 March 2008


PDB ID 1l9w

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands:
Activity: 3-dehydroquinate dehydratase, with EC number 4.2.1.10
Coordinates: save as pdb, mmCIF, xml



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. 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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