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1gck

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THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE

Structural highlights

1gck is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AAPAT_THET8 Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).^[1] ^[2] ^[3]

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

Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic substrates. During the course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently. The introduction of a mobile Arg292* residue into ttAspAT was the key step in the change to a "dual-substrate" enzyme. The substrate recognition mechanism of this thermostable "dual-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.

Substrate recognition mechanism of thermophilic dual-substrate enzyme.,Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S J Biochem. 2001 Jul;130(1):89-98. PMID:11432784^[4]

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

References

↑ Dornfeld C, Weisberg AJ, K C R, Dudareva N, Jelesko JG, Maeda HA. Phylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway. Plant Cell. 2014 Jul;26(7):3101-14. PMID:25070637 doi:10.1105/tpc.114.127407
↑ Giustini C, Graindorge M, Cobessi D, Crouzy S, Robin A, Curien G, Matringe M. Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase. FEBS J. 2019 Feb 16. doi: 10.1111/febs.14789. PMID:30771275 doi:http://dx.doi.org/10.1111/febs.14789
↑ Okamoto A, Kato R, Masui R, Yamagishi A, Oshima T, Kuramitsu S. An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. J Biochem. 1996 Jan;119(1):135-44. PMID:8907187 doi:10.1093/oxfordjournals.jbchem.a021198
↑ Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S. Substrate recognition mechanism of thermophilic dual-substrate enzyme. J Biochem. 2001 Jul;130(1):89-98. PMID:11432784

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gck"

@@ Line 3: / Line 3: @@
 <StructureSection load='1gck' size='340' side='right'caption='[[1gck]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gck]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GCK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gck]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GCK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bjw|1bjw]], [[1bkg|1bkg]], [[1b5p|1b5p]], [[1gc3|1gc3]], [[1gc4|1gc4]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=1gck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gck OCA], [https://pdbe.org/1gck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gck RCSB], [https://www.ebi.ac.uk/pdbsum/1gck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gck 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=1gck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gck OCA], [http://pdbe.org/1gck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gck RCSB], [http://www.ebi.ac.uk/pdbsum/1gck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gck ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/AAPAT_THET8 AAPAT_THET8] Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).<ref>PMID:25070637</ref> <ref>PMID:30771275</ref> <ref>PMID:8907187</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Aspartate transaminase]]
 [[Category: Large Structures]]
-[[Category: Hirotsu, K]]
+[[Category: Thermus thermophilus HB8]]
-[[Category: Kuramitsu, S]]
+[[Category: Hirotsu K]]
-[[Category: Nakai, T]]
+[[Category: Kuramitsu S]]
-[[Category: Ura, H]]
+[[Category: Nakai T]]
-[[Category: Aminotransferase]]
+[[Category: Ura H]]
-[[Category: Dual-substrate enzyme]]
-[[Category: Pyridoxal enzyme]]
-[[Category: Transferase]]

1gck

From Proteopedia

Current revision

THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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