4erg

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==Evidence for a Dual Role of an Active Site Histidine in alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde Decarboxylase==
==Evidence for a Dual Role of an Active Site Histidine in alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde Decarboxylase==
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<StructureSection load='4erg' size='340' side='right' caption='[[4erg]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
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<StructureSection load='4erg' size='340' side='right'caption='[[4erg]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4erg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ERG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ERG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4erg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ERG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ERG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.789&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4epk|4epk]], [[4era|4era]], [[4eri|4eri]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nbaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 Pseudomonas fluorescens])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4erg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erg OCA], [https://pdbe.org/4erg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4erg RCSB], [https://www.ebi.ac.uk/pdbsum/4erg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4erg ProSAT]</span></td></tr>
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<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=4erg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4erg RCSB], [http://www.ebi.ac.uk/pdbsum/4erg PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q83V25_PSEFL Q83V25_PSEFL]
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The previously reported crystal structures of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) show a five-coordinate Zn(II)(His)(3)(Asp)(OH(2)) active site. The water ligand is H-bonded to a conserved His228 residue adjacent to the metal center in ACMSD from Pseudomonas fluorescens (PfACMSD). Site-directed mutagenesis of His228 to tyrosine and glycine in this study results in a complete or significant loss of activity. Metal analysis shows that H228Y and H228G contain iron rather than zinc, indicating that this residue plays a role in the metal selectivity of the protein. As-isolated H228Y displays a blue color, which is not seen in wild-type ACMSD. Quinone staining and resonance Raman analyses indicate that the blue color originates from Fe(III)-tyrosinate ligand-to-metal charge transfer. Co(II)-substituted H228Y ACMSD is brown in color and exhibits an electron paramagnetic resonance spectrum showing a high-spin Co(II) center with a well-resolved (59)Co (I = (7)/(2)) eight-line hyperfine splitting pattern. The X-ray crystal structures of as-isolated Fe-H228Y (2.8 A) and Co-substituted (2.4 A) and Zn-substituted H228Y (2.0 A resolution) support the spectroscopic assignment of metal ligation of the Tyr228 residue. The crystal structure of Zn-H228G (2.6 A) was also determined. These four structures show that the water ligand present in WT Zn-ACMSD is either missing (Fe-H228Y, Co-H228Y, and Zn-H228G) or disrupted (Zn-H228Y) in response to the His228 mutation. Together, these results highlight the importance of His228 for PfACMSD's metal specificity as well as maintaining a water molecule as a ligand of the metal center. His228 is thus proposed to play a role in activating the metal-bound water ligand for subsequent nucleophilic attack on the substrate.
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Evidence for a Dual Role of an Active Site Histidine in alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde Decarboxylase.,Huo L, Fielding AJ, Chen Y, Li T, Iwaki H, Hosler JP, Chen L, Hasegawa Y, Que L Jr, Liu A Biochemistry. 2012 Jul 24;51(29):5811-21. Epub 2012 Jul 12. PMID:22746257<ref>PMID:22746257</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
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[[Category: Chen, L]]
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[[Category: Chen L]]
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[[Category: Chen, Y]]
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[[Category: Chen Y]]
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[[Category: Fielding, A J]]
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[[Category: Fielding AJ]]
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[[Category: Hasegawa, Y]]
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[[Category: Hasegawa Y]]
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[[Category: Hosler, J P]]
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[[Category: Hosler JP]]
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[[Category: Huo, L]]
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[[Category: Huo L]]
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[[Category: Iwaki, H]]
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[[Category: Iwaki H]]
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[[Category: Li, T]]
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[[Category: Li T]]
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[[Category: Liu, A]]
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[[Category: Liu A]]
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[[Category: Que, L]]
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[[Category: Que Jr L]]
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[[Category: Decarboxylase]]
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[[Category: Fe]]
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[[Category: Lyase]]
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[[Category: Metal-binding]]
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[[Category: Tim-barrel]]
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Current revision

Evidence for a Dual Role of an Active Site Histidine in alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde Decarboxylase

PDB ID 4erg

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