1a3g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:23, 5 June 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1a3g.png|left|200px]]
 
-
<!--
+
==BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI==
-
The line below this paragraph, containing "STRUCTURE_1a3g", creates the "Structure Box" on the page.
+
<StructureSection load='1a3g' size='340' side='right'caption='[[1a3g]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1a3g]] is a 3 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=1A3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A3G FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-
{{STRUCTURE_1a3g| PDB=1a3g | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a3g OCA], [https://pdbe.org/1a3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a3g RCSB], [https://www.ebi.ac.uk/pdbsum/1a3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a3g ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ILVE_ECOLI ILVE_ECOLI] Acts on leucine, isoleucine and valine.
 +
== 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/a3/1a3g_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=1a3g ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The X-ray crystallographic structure of the branched-chain amino acid aminotransferase from Escherichia coli was determined by means of isomorphous replacement using the selenomethionyl enzyme as one of the heavy atom derivatives. The enzyme is a homo hexamer with D3 symmetry, and the polypeptide chain of the subunit is folded into two domains (small and large domains). The coenzyme, pyridoxal 5'-phosphate, resides at the domain interface, its re-face facing toward the protein. The active site structure shows that the following sites can recognize branched-chain amino acids and glutamate as substrates: (1) a hydrophobic core formed by Phe36, Tyr164, Tyr31*, and Val109* for a branched-chain; (2) Arg97 for an acidic side chain of glutamate; and (3) Tyr95 and two main chain NH groups of Thr257 and Ala258 for the alpha-carboxylate of substrates. Although the main chain conformation of the active site is homologous to that of D-amino acid aminotransferase, many of the active site residues are different between them.
-
===BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI===
+
Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution.,Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H J Biochem. 1997 Apr;121(4):637-41. PMID:9163511<ref>PMID:9163511</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_9163511}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1a3g" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 9163511 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_9163511}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1A3G is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3G OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:9163511</ref><references group="xtra"/>
+
-
[[Category: Branched-chain-amino-acid transaminase]]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Hayashi, H.]]
+
[[Category: Large Structures]]
-
[[Category: Hirotsu, K.]]
+
[[Category: Hayashi H]]
-
[[Category: Kagamiyama, H.]]
+
[[Category: Hirotsu K]]
-
[[Category: Okada, K.]]
+
[[Category: Kagamiyama H]]
-
[[Category: Sato, M.]]
+
[[Category: Okada K]]
-
[[Category: Aminotransferase]]
+
[[Category: Sato M]]
-
[[Category: Pyridoxal enzyme]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:21:46 2009''
+

Current revision

BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI

PDB ID 1a3g

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools