2yqc: Difference between revisions
New page: left|200px<br /><applet load="2yqc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2yqc, resolution 1.90Å" /> '''Crystal Structure of... |
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[[Image:2yqc.gif|left|200px]]<br /><applet load="2yqc" size=" | [[Image:2yqc.gif|left|200px]]<br /><applet load="2yqc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2yqc, resolution 1.90Å" /> | caption="2yqc, resolution 1.90Å" /> | ||
'''Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the apo-like form'''<br /> | '''Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the apo-like form'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2YQC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans] with MG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 2YQC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YQC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: uridine-diphospho-n-acetylglucosamine]] | [[Category: uridine-diphospho-n-acetylglucosamine]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:48:03 2008'' | ||
Revision as of 15:48, 23 January 2008
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Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the apo-like form
OverviewOverview
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 Nacetylglucosamine-1-phopsphate, (GlcNAc-1-P) and uridine-5'-triphosphate (UTP) by UDPGlcNAc, pyrophosphorylase (UAP). This is SN2 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 UDPGlcNAc and acts as a co-factor. 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 StructureAbout this Structure
2YQC is a Single protein structure of sequence from Candida albicans with and as ligands. Active as UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23 Full crystallographic information is available from OCA.
ReferenceReference
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 Mar 28;. PMID:17392279
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