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5o9x

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Revision as of 07:48, 29 August 2018

Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutate S69A in complex with glucose1,6bisphosphate

Structural highlights

5o9x is a 1 chain structure with sequence from Aspergillus lentulus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	ALT_8497 (Aspergillus lentulus)
Activity:	Phosphoacetylglucosamine mutase, with EC number 5.4.2.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[A0A0S7E9S6_9EURO] Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.[PIRNR:PIRNR016408]

Publication Abstract from PubMed

N -acetylphosphoglucosamine mutase (AGM1) is a key component of the hexosamine biosynthetic pathway that produces UDP-GlcNAc, an essential precursor for a wide range of glycans in eukaryotes. AGM belongs to the a-D-phosphohexomutase metalloenzyme superfamily and catalyses the interconversion of N -acetylglucosamine-6-phosphate (GlcNAc-6P) to N -acetylglucosamine-1-phosphate (GlcNAc-1P) through N -acetylglucosamine-1,6-bisphosphate (GlcNAc-1,6-bisP) as the catalytic intermediate. Although there is an understanding of the phosphoserine-dependent catalytic mechanism at enzymatic and structural level, the identity of the requisite catalytic base in AGM1/phosphoglucomutases is as yet unknown. Here we present crystal structures of a Michaelis complex of AGM1 with GlcNAc-6P and Mg(2+), and a complex of the inactive Ser69Ala mutant together with glucose-1,6-bisphosphate (Glc-1,6-bisP) that represent key snapshots along the reaction coordinate. Together with mutagenesis, these structures reveal that the phosphate group of the hexose-1,6-bisP intermediate may act as the catalytic base.

Evidence for substrate assisted catalysis in N-acetylphosphoglucosamine mutase.,Raimi OG, Hurtado Guerrero R, van Aalten DM Biochem J. 2018 Jul 2. pii: BCJ20180172. doi: 10.1042/BCJ20180172. PMID:29967067^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Raimi OG, Hurtado Guerrero R, van Aalten DM. Evidence for substrate assisted catalysis in N-acetylphosphoglucosamine mutase. Biochem J. 2018 Jul 2. pii: BCJ20180172. doi: 10.1042/BCJ20180172. PMID:29967067 doi:http://dx.doi.org/10.1042/BCJ20180172

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5o9x"

@@ Line 3: / Line 3: @@
 <StructureSection load='5o9x' size='340' side='right' caption='[[5o9x]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5o9x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O9X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5o9x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_lentulus Aspergillus lentulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O9X FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALT_8497 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=293939 Aspergillus lentulus])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoacetylglucosamine_mutase Phosphoacetylglucosamine mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.3 5.4.2.3] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5o9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9x OCA], [http://pdbe.org/5o9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o9x RCSB], [http://www.ebi.ac.uk/pdbsum/5o9x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9x ProSAT]</span></td></tr>
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Aspergillus lentulus]]
 [[Category: Phosphoacetylglucosamine mutase]]
 [[Category: Hurtado-Guerrero, R]]

5o9x

From Proteopedia

Revision as of 07:48, 29 August 2018

Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutate S69A in complex with glucose1,6bisphosphate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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