1sg6
From Proteopedia
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| - | [[Image:1sg6.gif|left|200px]] | + | [[Image:1sg6.gif|left|200px]] |
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| - | '''Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D''' | + | {{Structure |
| + | |PDB= 1sg6 |SIZE=350|CAPTION= <scene name='initialview01'>1sg6</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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, AROM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=162425 Emericella nidulans]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SG6 is a [ | + | 1SG6 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=1SG6 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover., Nichols CE, Hawkins AR, Stammers DK, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):971-3. Epub 2004, Apr 21. PMID:[http:// | + | Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover., Nichols CE, Hawkins AR, Stammers DK, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):971-3. Epub 2004, Apr 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103156 15103156] |
[[Category: 3-dehydroquinate synthase]] | [[Category: 3-dehydroquinate synthase]] | ||
[[Category: Emericella nidulans]] | [[Category: Emericella nidulans]] | ||
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[[Category: aromatic amino acid biosynthesis]] | [[Category: aromatic amino acid biosynthesis]] | ||
[[Category: cyclase]] | [[Category: cyclase]] | ||
| - | [[Category: | + | [[Category: dhq]] |
[[Category: domain movement]] | [[Category: domain movement]] | ||
[[Category: form j]] | [[Category: form j]] | ||
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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 14:04:30 2008'' |
Revision as of 12:04, 20 March 2008
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| , resolution 1.7Å | |||||||
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| Ligands: | and | ||||||
| Gene: | AROMA, AROM (Emericella nidulans) | ||||||
| Activity: | 3-dehydroquinate synthase, with EC number 4.2.3.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D
Overview
Crystallization of Aspergillus nidulans 3-dehydroquinate synthase (DHQS), following turnover of the enzyme by addition of the substrate DAHP, gave a new crystal form (form J). Although the crystals have dimensions of only 50 x 20 x 5 micro m, they are well ordered, diffracting to 1.7 A. The space group is C222(1), with unit-cell parameters a = 90.0, b = 103.7, c = 177.4 A. Structure determination and refinement to R = 0.19 (R(free) = 0.25) shows the DHQS is in the 'open' form with the substrate site unoccupied but with some loop regions perturbed. Previous crystals of open-form DHQS only diffracted to 2.5 A resolution. The use of enzyme turnover may be applicable in other systems in attempts to improve crystal quality.
About this Structure
1SG6 is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.
Reference
Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover., Nichols CE, Hawkins AR, Stammers DK, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):971-3. Epub 2004, Apr 21. PMID:15103156
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