1wcq

From Proteopedia

(Difference between revisions)

Revision as of 16:18, 27 October 2021

Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine.

Structural highlights

1wcq is a 3 chain structure with sequence from "micromonospora_viridifaciens"_routien "micromonospora viridifaciens" routien. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1eur, 1eus, 1eut, 1euu, 1w8n, 1w8o
Activity:	Exo-alpha-sialidase, with EC number 3.2.1.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NANH_MICVI] To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Mutants of the Micromonospora viridifaciens sialidase, Y370E and Y370F, are catalytically active retaining enzymes that operate by different mechanisms. Previous substitutions with smaller amino acids, including Y370D, yielded inverting sialidases. At least one water molecule can fit into the active-site cavity of this mutant and act as a nucleophile from the face opposite the leaving group (Biochemistry 2003, 42, 12 682). Thus, addition of a CH(2) unit (Asp versus Glu) changes the mechanism from inversion back to retention of configuration. Based on Bronsted beta(lg) values, it is proposed that the Y370E mutant reacts by a double-displacement mechanism (beta(lg) on k(cat)/K(m) -0.36+/-0.04) with Glu370 acting as the nucleophile. However, the Y370F mutant (beta(lg) on k(cat)/K(m) -0.79+/-0.12) reacts via a dissociative transition state. The crystal structure of the Y370F mutant complexed with 2-deoxy-2,3-dehydro-N-acetylneuraminic acid shows no significant active-site perturbation relative to the wild-type enzyme.

Two nucleophilic mutants of the Micromonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms.,Watson JN, Newstead S, Narine AA, Taylor G, Bennet AJ Chembiochem. 2005 Nov;6(11):1999-2004. PMID:16206228^[1]

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

References

↑ Watson JN, Newstead S, Narine AA, Taylor G, Bennet AJ. Two nucleophilic mutants of the Micromonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms. Chembiochem. 2005 Nov;6(11):1999-2004. PMID:16206228 doi:10.1002/cbic.200500114

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wcq"

@@ Line 3: / Line 3: @@
 <StructureSection load='1wcq' size='340' side='right'caption='[[1wcq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wcq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"micromonospora_viridifaciens"_routien "micromonospora viridifaciens" routien]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WCQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wcq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"micromonospora_viridifaciens"_routien "micromonospora viridifaciens" routien]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WCQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eur|1eur]], [[1eus|1eus]], [[1eut|1eut]], [[1euu|1euu]], [[1w8n|1w8n]], [[1w8o|1w8o]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eur|1eur]], [[1eus|1eus]], [[1eut|1eut]], [[1euu|1euu]], [[1w8n|1w8n]], [[1w8o|1w8o]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=1wcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wcq OCA], [http://pdbe.org/1wcq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wcq RCSB], [http://www.ebi.ac.uk/pdbsum/1wcq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wcq ProSAT]</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=1wcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wcq OCA], [https://pdbe.org/1wcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wcq RCSB], [https://www.ebi.ac.uk/pdbsum/1wcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wcq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NANH_MICVI NANH_MICVI]] To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.
+[[https://www.uniprot.org/uniprot/NANH_MICVI NANH_MICVI]] To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Sialidase|Sialidase]]
+*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
 == References ==
 <references/>

1wcq

From Proteopedia

Revision as of 16:18, 27 October 2021

Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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