2v5j: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /> <applet load="2v5j" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v5j, resolution 1.60Å" /> '''APO CLASS II ALDOLA... |
No edit summary |
||
| (21 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Apo Class II aldolase HpcH== | ||
Microorganisms are adept at degrading chemically resistant aromatic | <StructureSection load='2v5j' size='340' side='right'caption='[[2v5j]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2v5j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_C Escherichia coli C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5J FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=2v5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5j OCA], [https://pdbe.org/2v5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5j RCSB], [https://www.ebi.ac.uk/pdbsum/2v5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5j ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HPCH_ECOLX HPCH_ECOLX] Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinate semialdehyde. Is also able to catalyze the aldol cleavage of 4-hydroxy-2-ketopentanoate and 4-hydroxy-2-ketohexanoate. Is not stereospecific since it can cleave both substrate enantiomers. Also exhibits significant oxaloacetate decarboxylase activity in vitro. In the reverse direction, is able to condense a range of aldehyde acceptors (from two to five carbons in length) with pyruvate or 2-oxobutanoate. Unlike with BphI from Burkholderia xenovorans, the aldol addition reaction lacks stereospecificity, producing a racemic mixture.<ref>PMID:15996099</ref> <ref>PMID:20364820</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/2v5j_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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=2v5j ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Microorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class II aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 A and 2.0 A, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues. | |||
Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli.,Rea D, Fulop V, Bugg TD, Roper DI J Mol Biol. 2007 Nov 2;373(4):866-76. Epub 2007 Jun 26. PMID:17881002<ref>PMID:17881002</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2v5j" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aldolase 3D structures|Aldolase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli C]] | |||
[[Category: Large Structures]] | |||
[[Category: Bugg TDH]] | |||
[[Category: Fulop V]] | |||
[[Category: Rea D]] | |||
[[Category: Roper DI]] | |||
Latest revision as of 18:06, 13 December 2023
Apo Class II aldolase HpcHApo Class II aldolase HpcH
Structural highlights
FunctionHPCH_ECOLX Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinate semialdehyde. Is also able to catalyze the aldol cleavage of 4-hydroxy-2-ketopentanoate and 4-hydroxy-2-ketohexanoate. Is not stereospecific since it can cleave both substrate enantiomers. Also exhibits significant oxaloacetate decarboxylase activity in vitro. In the reverse direction, is able to condense a range of aldehyde acceptors (from two to five carbons in length) with pyruvate or 2-oxobutanoate. Unlike with BphI from Burkholderia xenovorans, the aldol addition reaction lacks stereospecificity, producing a racemic mixture.[1] [2] 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 PubMedMicroorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class II aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 A and 2.0 A, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues. Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli.,Rea D, Fulop V, Bugg TD, Roper DI J Mol Biol. 2007 Nov 2;373(4):866-76. Epub 2007 Jun 26. PMID:17881002[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||