5hhf: Difference between revisions

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<StructureSection load='5hhf' size='340' side='right'caption='[[5hhf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5hhf' size='340' side='right'caption='[[5hhf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5hhf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HHF FirstGlance]. <br>
<table><tr><td colspan='2'>[[5hhf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HHF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=62F:[[(2~{R},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+[(2~{R},3~{S},4~{S})-5-[5-[(2~{R},3~{R},4~{S},5~{R},6~{R})-6-(HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]-7,8-DIMETHYL-2,4-BIS(OXIDANYL)BENZO[G]PTERIDIN-10-YL]-2,3,4-TRIS(OXIDANYL)PENTYL]+HYDROGEN+PHOSPHATE'>62F</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glf, glfA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746128 ASPFM])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=62F:[[(2~{R},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+[(2~{R},3~{S},4~{S})-5-[5-[(2~{R},3~{R},4~{S},5~{R},6~{R})-6-(HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]-7,8-DIMETHYL-2,4-BIS(OXIDANYL)BENZO[G]PTERIDIN-10-YL]-2,3,4-TRIS(OXIDANYL)PENTYL]+HYDROGEN+PHOSPHATE'>62F</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-galactopyranose_mutase UDP-galactopyranose mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.9 5.4.99.9] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hhf OCA], [https://pdbe.org/5hhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hhf RCSB], [https://www.ebi.ac.uk/pdbsum/5hhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hhf ProSAT]</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=5hhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hhf OCA], [http://pdbe.org/5hhf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hhf RCSB], [http://www.ebi.ac.uk/pdbsum/5hhf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hhf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q4W1X2_ASPFM Q4W1X2_ASPFM]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[UDP-galactopyranose mutase|UDP-galactopyranose mutase]]
*[[UDP-galactopyranose mutase 3D structures|UDP-galactopyranose mutase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aspfm]]
[[Category: Aspergillus fumigatus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: UDP-galactopyranose mutase]]
[[Category: Tanner JJ]]
[[Category: Tanner, J J]]
[[Category: Covalent reaction intermediate]]
[[Category: Flavin adenine dinucleotide binding]]
[[Category: Isomerase]]
[[Category: Mutase]]
[[Category: Nucleotide binding]]

Latest revision as of 10:36, 9 August 2023

Crystal structure of Aspergillus fumigatus UDP-Galactopyranose mutase mutant H63A with covalent FAD-Galactopyranose and bound UDPCrystal structure of Aspergillus fumigatus UDP-Galactopyranose mutase mutant H63A with covalent FAD-Galactopyranose and bound UDP

Structural highlights

5hhf is a 4 chain structure with sequence from Aspergillus fumigatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q4W1X2_ASPFM

Publication Abstract from PubMed

UDP-galactopyranose mutase (UGM) plays an essential role in galactofuranose biosynthesis in pathogens by catalyzing the conversion of UDP-galactopyranose to UDP-galactofuranose. Here we report the first crystal structure of a covalent intermediate in the UGM reaction. The 2.3 A resolution structure reveals UDP bound in the active site and galactopyranose linked to the FAD through a covalent bond between the anomeric C of galactopyranose and N5 of the FAD. The structure confirms the role of the flavin as nucleophile and supports the hypothesis that the proton destined for O5 of galactofuranose is shuttled from N5 of the FAD via O4 of the FAD.

In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction.,Mehra-Chaudhary R, Dai Y, Sobrado P, Tanner JJ Biochemistry. 2016 Feb 16;55(6):833-6. doi: 10.1021/acs.biochem.6b00035. Epub, 2016 Feb 4. PMID:26836146[1]

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

See Also

References

  1. ↑ Mehra-Chaudhary R, Dai Y, Sobrado P, Tanner JJ. In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction. Biochemistry. 2016 Feb 16;55(6):833-6. doi: 10.1021/acs.biochem.6b00035. Epub, 2016 Feb 4. PMID:26836146 doi:http://dx.doi.org/10.1021/acs.biochem.6b00035

5hhf, resolution 2.30Å

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