3laz: Difference between revisions

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==The crystal structure of the N-terminal domain of D-galactarate dehydratase from Escherichia coli CFT073==
==The crystal structure of the N-terminal domain of D-galactarate dehydratase from Escherichia coli CFT073==
<StructureSection load='3laz' size='340' side='right' caption='[[3laz]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
<StructureSection load='3laz' size='340' side='right'caption='[[3laz]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3laz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecol6 Ecol6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LAZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3laz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LAZ FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.921&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">c3883, yhaG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=199310 ECOL6])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactarate_dehydratase Galactarate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.42 4.2.1.42] </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=3laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3laz OCA], [https://pdbe.org/3laz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3laz RCSB], [https://www.ebi.ac.uk/pdbsum/3laz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3laz 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=3laz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3laz OCA], [http://pdbe.org/3laz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3laz RCSB], [http://www.ebi.ac.uk/pdbsum/3laz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3laz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GARD_ECOLI GARD_ECOLI] Catalyzes the dehydration of galactarate to form 5-dehydro-4-deoxy-D-glucarate.[HAMAP-Rule:MF_02031]<ref>PMID:9772162</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/3laz_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/3laz_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3laz ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3laz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecol6]]
[[Category: Escherichia coli CFT073]]
[[Category: Galactarate dehydratase]]
[[Category: Large Structures]]
[[Category: Bearden, J]]
[[Category: Bearden J]]
[[Category: Joachimiak, A]]
[[Category: Joachimiak A]]
[[Category: Li, H]]
[[Category: Li H]]
[[Category: Structural genomic]]
[[Category: Tan K]]
[[Category: Tan, K]]
[[Category: Lyase]]
[[Category: Mcsg]]
[[Category: PSI, Protein structure initiative]]

Latest revision as of 12:23, 30 October 2024

The crystal structure of the N-terminal domain of D-galactarate dehydratase from Escherichia coli CFT073The crystal structure of the N-terminal domain of D-galactarate dehydratase from Escherichia coli CFT073

Structural highlights

3laz is a 2 chain structure with sequence from Escherichia coli CFT073. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.921Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GARD_ECOLI Catalyzes the dehydration of galactarate to form 5-dehydro-4-deoxy-D-glucarate.[HAMAP-Rule:MF_02031][1]

Evolutionary Conservation

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

References

  1. Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry. 1998 Oct 13;37(41):14369-75. PMID:9772162 doi:http://dx.doi.org/10.1021/bi981124f

3laz, resolution 1.92Å

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OCA