3fvu

From Proteopedia

(Difference between revisions)

Revision as of 08:12, 2 March 2022

Crystal Structure of Human Kynurenine Aminotransferase I in Complex with Indole-3-acetic Acid

Structural highlights

3fvu is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	3fvs
Gene:	CCBL1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KAT1_HUMAN] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.^[1]

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 PubMed

Human kynurenine aminotransferase I (hKAT I) catalyzes the formation of kynurenic acid, a neuroactive compound. Here, we report three high-resolution crystal structures (1.50-1.55 A) of hKAT I that are in complex with glycerol and each of two inhibitors of hKAT I: indole-3-acetic acid (IAC) and Tris. Because Tris is able to occupy the substrate binding position, we speculate that this may be the basis for hKAT I inhibition. Furthermore, the hKAT/IAC complex structure reveals that the binding moieties of the inhibitor are its indole ring and a carboxyl group. Six chemicals with both binding moieties were tested for their ability to inhibit hKAT I activity; 3-indolepropionic acid and DL-indole-3-lactic acid demonstrated the highest level of inhibition, and as they cannot be considered as substrates of the enzyme, these two inhibitors are promising candidates for future study. Perhaps even more significantly, we report the discovery of two different ligands located simultaneously in the hKAT I active center for the first time.

Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K.,Han Q, Robinson H, Cai T, Tagle DA, Li J J Med Chem. 2009 May 14;52(9):2786-93. PMID:19338303^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Han Q, Robinson H, Cai T, Tagle DA, Li J. Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K. J Med Chem. 2009 May 14;52(9):2786-93. PMID:19338303 doi:10.1021/jm9000874
↑ Han Q, Robinson H, Cai T, Tagle DA, Li J. Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K. J Med Chem. 2009 May 14;52(9):2786-93. PMID:19338303 doi:10.1021/jm9000874

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3fvu"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Human Kynurenine Aminotransferase I in Complex with Indole-3-acetic Acid==
-<StructureSection load='3fvu' size='340' side='right' caption='[[3fvu]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='3fvu' size='340' side='right'caption='[[3fvu]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3fvu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FVU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FVU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3fvu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FVU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IAC:1H-INDOL-3-YLACETIC+ACID'>IAC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</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=IAC:1H-INDOL-3-YLACETIC+ACID'>IAC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fvs|3fvs]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fvs|3fvs]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCBL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCBL1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3fvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fvu OCA], [http://pdbe.org/3fvu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fvu RCSB], [http://www.ebi.ac.uk/pdbsum/3fvu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fvu ProSAT]</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=3fvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fvu OCA], [https://pdbe.org/3fvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fvu RCSB], [https://www.ebi.ac.uk/pdbsum/3fvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fvu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.<ref>PMID:19338303</ref>
+[[https://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.<ref>PMID:19338303</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Cai, T]]
 [[Category: Han, Q]]

3fvu

From Proteopedia

Revision as of 08:12, 2 March 2022

Crystal Structure of Human Kynurenine Aminotransferase I in Complex with Indole-3-acetic Acid

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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