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==Crystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and L-tartrate==
==Crystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and L-tartrate==
<StructureSection load='3v4b' size='340' side='right' caption='[[3v4b]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='3v4b' size='340' side='right'caption='[[3v4b]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3v4b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Celju Celju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V4B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V4B FirstGlance]. <br>
<table><tr><td colspan='2'>[[3v4b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus_Ueda107 Cellvibrio japonicus Ueda107]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V4B 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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]] 1.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v3w|3v3w]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rspA, CJA_3069 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=498211 CELJU])</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=3v4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4b OCA], [https://pdbe.org/3v4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v4b RCSB], [https://www.ebi.ac.uk/pdbsum/3v4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4b 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=3v4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4b OCA], [http://pdbe.org/3v4b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v4b RCSB], [http://www.ebi.ac.uk/pdbsum/3v4b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MAND_CELJU MAND_CELJU]] Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref>
[https://www.uniprot.org/uniprot/MAND_CELJU MAND_CELJU] Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref>  
 
==See Also==
*[[Enolase 3D structures|Enolase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Celju]]
[[Category: Cellvibrio japonicus Ueda107]]
[[Category: Almo, S C]]
[[Category: Large Structures]]
[[Category: Bhosle, R]]
[[Category: Al Obaidi N]]
[[Category: Chowdhury, S]]
[[Category: Almo SC]]
[[Category: EFI, Enzyme Function Initiative]]
[[Category: Bhosle R]]
[[Category: Evans, B]]
[[Category: Chowdhury S]]
[[Category: Gerlt, J A]]
[[Category: Evans B]]
[[Category: Glenn, A Scott]]
[[Category: Gerlt JA]]
[[Category: Hammonds, J]]
[[Category: Hammonds J]]
[[Category: Hillerich, B]]
[[Category: Hillerich B]]
[[Category: Imker, H J]]
[[Category: Imker HJ]]
[[Category: Morisco, L L]]
[[Category: Morisco LL]]
[[Category: Obaidi, N Al]]
[[Category: Scott Glenn A]]
[[Category: Seidel, R D]]
[[Category: Seidel RD]]
[[Category: Sojitra, S]]
[[Category: Sojitra S]]
[[Category: Toro, R]]
[[Category: Toro R]]
[[Category: Vetting, M W]]
[[Category: Vetting MW]]
[[Category: Washington, E]]
[[Category: Washington E]]
[[Category: Wasserman, S R]]
[[Category: Wasserman SR]]
[[Category: Zencheck, W D]]
[[Category: Zencheck WD]]
[[Category: Efi]]
[[Category: Enolase]]
[[Category: Enzyme function initiative]]
[[Category: Lyase]]

Latest revision as of 17:17, 14 March 2024

Crystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and L-tartrateCrystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET EFI-502161) with bound MG and L-tartrate

Structural highlights

3v4b is a 1 chain structure with sequence from Cellvibrio japonicus Ueda107. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAND_CELJU Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).[1]

See Also

References

  1. ↑ Wichelecki DJ, Balthazor BM, Chau AC, Vetting MW, Fedorov AA, Fedorov EV, Lukk T, Patskovsky YV, Stead MB, Hillerich BS, Seidel RD, Almo SC, Gerlt JA. Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the D-mannonate dehydratase subgroup. Biochemistry. 2014 Apr 29;53(16):2722-31. doi: 10.1021/bi500264p. Epub 2014 Apr, 15. PMID:24697546 doi:http://dx.doi.org/10.1021/bi500264p

3v4b, resolution 1.40Å

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