1nvf: Difference between revisions
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'''Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, ADP and carbaphosphonate''' | {{Structure | ||
|PDB= 1nvf |SIZE=350|CAPTION= <scene name='initialview01'>1nvf</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=CRB:[1R-(1ALPHA,3BETA,4ALPHA,5BETA)]-5-(PHOSPHONOMETHYL)-1,3,4-TRIHYDROXYCYCLOHEXANE-1-CARBOXYLIC ACID'>CRB</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/3-dehydroquinate_synthase 3-dehydroquinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.4 4.2.3.4] | |||
|GENE= AROMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=162425 Emericella nidulans]) | |||
}} | |||
'''Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, ADP and carbaphosphonate''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NVF is a [ | 1NVF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NVF OCA]. | ||
==Reference== | ==Reference== | ||
Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase., Nichols CE, Ren J, Lamb HK, Hawkins AR, Stammers DK, J Mol Biol. 2003 Mar 14;327(1):129-44. PMID:[http:// | Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase., Nichols CE, Ren J, Lamb HK, Hawkins AR, Stammers DK, J Mol Biol. 2003 Mar 14;327(1):129-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12614613 12614613] | ||
[[Category: 3-dehydroquinate synthase]] | [[Category: 3-dehydroquinate synthase]] | ||
[[Category: Emericella nidulans]] | [[Category: Emericella nidulans]] | ||
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[[Category: closed form]] | [[Category: closed form]] | ||
[[Category: cyclase]] | [[Category: cyclase]] | ||
[[Category: | [[Category: dhq]] | ||
[[Category: domain movement]] | [[Category: domain movement]] | ||
[[Category: form h]] | [[Category: form h]] | ||
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[[Category: shikimate pathway]] | [[Category: shikimate pathway]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:02:16 2008'' | ||
Revision as of 14:02, 20 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | AROMA (Emericella nidulans) | ||||||
| Activity: | 3-dehydroquinate synthase, with EC number 4.2.3.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, ADP and carbaphosphonate
OverviewOverview
In order to investigate systematically substrate and cofactor-induced conformational changes in the enzyme dehydroquinate synthase (DHQS), eight structures representing a series of differently liganded states have been determined in a total of six crystal forms. DHQS in the absence of the substrate analogue carbaphosphonate, either unliganded or in the presence of NAD or ADP, is in an open form where a relative rotation of 11-13 degrees between N and C-terminal domains occurs.Analysis of torsion angle difference plots between sets of structures reveals eight rearrangements that appear relevant to domain closure and a further six related to crystal packing. Overlapping 21 different copies of the individual N and C-terminal DHQS domains further reveals a series of pivot points about which these movements occur and illustrates the way in which widely separated secondary structure elements are mechanically inter-linked to form "composite elements", which propagate structural changes across large distances.This analysis has provided insight into the basis of DHQS ligand-initiated domain closure and gives rise to the proposal of an ordered sequence of events involving substrate binding, and local rearrangements within the active site that are propagated to the hinge regions, leading to closure of the active-site cleft.
About this StructureAbout this Structure
1NVF is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.
ReferenceReference
Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase., Nichols CE, Ren J, Lamb HK, Hawkins AR, Stammers DK, J Mol Biol. 2003 Mar 14;327(1):129-44. PMID:12614613
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