This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3qpg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:48, 21 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3qpg' size='340' side='right'caption='[[3qpg]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
<StructureSection load='3qpg' size='340' side='right'caption='[[3qpg]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3qpg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPG FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3qpg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPG FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3QP:(E)-N-{2-HYDROXY-3-METHYL-6-[(PHOSPHONOOXY)METHYL]BENZYLIDENE}-L-ASPARTIC+ACID'>3QP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.79&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qn6|3qn6]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3QP:(E)-N-{2-HYDROXY-3-METHYL-6-[(PHOSPHONOOXY)METHYL]BENZYLIDENE}-L-ASPARTIC+ACID'>3QP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [https://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=3qpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpg OCA], [https://pdbe.org/3qpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpg RCSB], [https://www.ebi.ac.uk/pdbsum/3qpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpg 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=3qpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpg OCA], [https://pdbe.org/3qpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpg RCSB], [https://www.ebi.ac.uk/pdbsum/3qpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpg ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
-
The 1.8 A resolution crystal structures of Escherichia coli aspartate aminotransferase reconstituted with 1-deazapyridoxal 5'-phosphate (deazaPLP; 2-formyl-3-hydroxy-4-methylbenzyl phosphate) in the internal aldimine and l-aspartate external aldimine forms are reported. The l-aspartate.deazaPLP external aldimine is extraordinarily stable (half-life of &gt;20 days), allowing crystals of this intermediate to be grown by cocrystallization with l-aspartate. This structure is compared to that of the alpha-methyl-l-aspartate.PLP external aldimine. Overlays with the corresponding pyridoxal 5'-phosphate (PLP) aldimines show very similar orientations of deazaPLP with respect to PLP. The lack of a hydrogen bond between Asp222 and deazaPLP, which serves to "anchor" PLP in the active site, releases strain in the deazaPLP internal aldimine that is enforced in the PLP internal aldimine [Hayashi, H., Mizuguchi, H., Miyahara, I., Islam, M. M., Ikushiro, H., Nakajima, Y., Hirotsu, K., and Kagamiyama, H. (2003) Biochim. Biophys. Acta1647, 103] as evidenced by the planarity of the pyridine ring and the Schiff base linkage with Lys258. Additionally, loss of this anchor causes a 10 degrees greater tilt of deazaPLP toward the substrate in the external aldimine. An important mechanistic difference between the l-aspartate.deazaPLP and alpha-methyl-l-aspartate.PLP external aldimines is a hydrogen bond between Gly38 and Lys258 in the former, positioning the catalytic base above and approximately equidistant between Calpha and C4'. In contrast, in the alpha-methyl-l-aspartate.PLP external aldimine, the epsilon-amino group of Lys258 is rotated approximately 70 degrees to form a hydrogen bond to Tyr70 because of the steric bulk of the methyl group.
+
-
 
+
-
Crystal Structures of Aspartate Aminotransferase Reconstituted with 1-Deazapyridoxal 5'-Phosphate: Internal Aldimine and Stable l-Aspartate External Aldimine.,Griswold WR, Fisher AJ, Toney MD Biochemistry. 2011 Jun 9. PMID:21627105<ref>PMID:21627105</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3qpg" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bacillus coli migula 1895]]
+
[[Category: Escherichia coli]]
-
[[Category: Aspartate transaminase]]
+
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Griswold, W R]]
+
[[Category: Griswold WR]]
-
[[Category: Aminotransferase]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal Structures of Escherichia coli Aspartate Aminotransferase Reconstituted with 1-Deaza-Pyridoxal 5'-Phosphate: Internal Aldimine and Stable L-Aspartate External Aldimine

PDB ID 3qpg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3qpg"
Personal tools