1w8o

From Proteopedia

(Difference between revisions)

Revision as of 13:34, 13 October 2021

Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens

Structural highlights

1w8o is a 1 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
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

A recombinant D92G mutant sialidase from Micromonospora viridifaciens has been cloned, expressed and purified. Kinetic studies reveal that the replacement of the conserved aspartic acid with glycine results in a catalytically competent retaining sialidase that possesses significant activity against activated substrates. The contribution of this aspartate residue to the free energy of hydrolysis for natural substrates is greater than 19 kJ/mol. The three dimensional structure of the D92G mutant shows that the removal of aspartic acid 92 causes no significant re-arrangement of the active site, and that an ordered water molecule substitutes for the carboxylate group of D92.

Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens.,Watson JN, Newstead S, Dookhun V, Taylor G, Bennet AJ FEBS Lett. 2004 Nov 5;577(1-2):265-9. PMID:15527797^[1]

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

References

↑ Watson JN, Newstead S, Dookhun V, Taylor G, Bennet AJ. Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens. FEBS Lett. 2004 Nov 5;577(1-2):265-9. PMID:15527797 doi:10.1016/j.febslet.2004.10.016

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/1w8o"

@@ Line 3: / Line 3: @@
 <StructureSection load='1w8o' size='340' side='right'caption='[[1w8o]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1w8o]] is a 1 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=1W8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W8O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1w8o]] is a 1 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=1W8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W8O FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LBT:ALPHA-LACTOSE'>LBT</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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]]</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]]</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=1w8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w8o OCA], [http://pdbe.org/1w8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w8o RCSB], [http://www.ebi.ac.uk/pdbsum/1w8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w8o 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=1w8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w8o OCA], [https://pdbe.org/1w8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w8o RCSB], [https://www.ebi.ac.uk/pdbsum/1w8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w8o 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/>

1w8o

From Proteopedia

Revision as of 13:34, 13 October 2021

Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens

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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