4d9i: Difference between revisions

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<StructureSection load='4d9i' size='340' side='right'caption='[[4d9i]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4d9i' size='340' side='right'caption='[[4d9i]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4d9i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D9I FirstGlance]. <br>
<table><tr><td colspan='2'>[[4d9i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D9I FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 2&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d9g|4d9g]], [[4d9k|4d9k]], [[4d9m|4d9m]], [[4d9n|4d9n]]</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=4d9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d9i OCA], [https://pdbe.org/4d9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d9i RCSB], [https://www.ebi.ac.uk/pdbsum/4d9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d9i ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2871, JW2839, ygeX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diaminopropionate_ammonia-lyase Diaminopropionate ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.15 4.3.1.15] </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=4d9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d9i OCA], [http://pdbe.org/4d9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d9i RCSB], [http://www.ebi.ac.uk/pdbsum/4d9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d9i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DPAL_ECOLI DPAL_ECOLI]] Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta-Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them.<ref>PMID:12596860</ref> <ref>PMID:12821154</ref> <ref>PMID:22904288</ref> <ref>PMID:22505717</ref>
[https://www.uniprot.org/uniprot/DPAL_ECOLI DPAL_ECOLI] Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta-Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them.<ref>PMID:12596860</ref> <ref>PMID:12821154</ref> <ref>PMID:22904288</ref> <ref>PMID:22505717</ref>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Diaminopropionate ammonia-lyase]]
[[Category: Escherichia coli K-12]]
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bharath, S R]]
[[Category: Bharath SR]]
[[Category: Bisht, S]]
[[Category: Bisht S]]
[[Category: Murthy, M R.N]]
[[Category: Murthy MRN]]
[[Category: Rajaram, V]]
[[Category: Rajaram V]]
[[Category: Fold type ii plp-dependent enzyme]]
[[Category: Lyase]]
[[Category: Tryptophan synthase beta subunit-like plp-dependent enzymes superfamily]]

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