2yqh
From Proteopedia
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|PDB= 2yqh |SIZE=350|CAPTION= <scene name='initialview01'>2yqh</scene>, resolution 2.30Å | |PDB= 2yqh |SIZE=350|CAPTION= <scene name='initialview01'>2yqh</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=GN1:2-(ACETYLAMINO)-2-DEOXY-1-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE'>GN1</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GN1:2-(ACETYLAMINO)-2-DEOXY-1-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE'>GN1</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2yqc|2YQC]], [[2yqj|2YQJ]], [[2yqs|2YQS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yqh OCA], [http://www.ebi.ac.uk/pdbsum/2yqh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2yqh RCSB]</span> | ||
}} | }} | ||
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[[Category: Nishitani, Y.]] | [[Category: Nishitani, Y.]] | ||
[[Category: Nonaka, T.]] | [[Category: Nonaka, T.]] | ||
| - | [[Category: GN1]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SO4]] | ||
[[Category: candida albican]] | [[Category: candida albican]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: uridine-diphospho-n-acetylglucosamine]] | [[Category: uridine-diphospho-n-acetylglucosamine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:14:29 2008'' |
Revision as of 02:14, 31 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23 | ||||||
| Related: | 2YQC, 2YQJ, 2YQS
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the substrate-binding form
Overview
Uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc) is a precursor of the bacterial and fungal cell wall. It is also used in a component of N-linked glycosylation and the glycosylphosphoinositol anchor of eukaryotic proteins. It is synthesized from N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and uridine-5'-triphosphate (UTP) by UDP-GlcNAc pyrophosphorylase (UAP). This is an S(N)2 reaction; the non-esterified oxygen atom of the GlcNAc-1-P phosphate group attacks the alpha-phosphate group of UTP. We determined crystal structures of UAP from Candida albicans (CaUAP1) without any ligands and also complexed with its substrate or with its product. The series of structures in different forms shows the induced fit movements of CaUAP1. Three loops approaching the ligand molecule close the active site when ligand is bound. In addition, Lys-421, instead of the metal ion in prokaryotic UAPs, is coordinated by both phosphate groups of UDP-Glc-NAc and acts as a cofactor. However, a magnesium ion enhances the enzymatic activity of CaUAP1, and thus we propose that the magnesium ion increases the affinity between UTP and the enzyme by coordinating to the alpha- and gamma-phosphate group of UTP.
About this Structure
2YQH is a Single protein structure of sequence from Candida albicans. Full crystallographic information is available from OCA.
Reference
Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans and catalytic reaction mechanism., Maruyama D, Nishitani Y, Nonaka T, Kita A, Fukami TA, Mio T, Yamada-Okabe H, Yamada-Okabe T, Miki K, J Biol Chem. 2007 Jun 8;282(23):17221-30. Epub 2007 Mar 28. PMID:17392279
Page seeded by OCA on Mon Mar 31 05:14:29 2008
Categories: Candida albicans | Single protein | UDP-N-acetylglucosamine diphosphorylase | Kita, A. | Maruyama, D. | Miki, K. | Nishitani, Y. | Nonaka, T. | Candida albican | Crystal structure | N-acetylglucosamine | N-acetylglucosamine-1-phosphate | Pyrophosphorylase | Uridine-diphospho-n-acetylglucosamine
