1c9c: Difference between revisions

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New page: left|200px<br /><applet load="1c9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9c, resolution 2.4Å" /> '''ASPARTATE AMINOTRANSF...
 
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[[Image:1c9c.jpg|left|200px]]<br /><applet load="1c9c" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1c9c, resolution 2.4&Aring;" />
'''ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE'''<br />


==Overview==
==ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE==
Domain movement is sometimes essential for substrate recognition by an, enzyme. X-ray crystallography of aminotransferase with a series of, aliphatic substrates showed that the domain movement of aspartate, aminotransferase was changed dramatically from an open to a closed form by, the addition of only one CH(2) to the side chain of the C4 substrate, CH(3)(CH(2))C((alpha))H(NH(3)(+))COO(-). These crystallographic results, and reaction kinetics (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63;, Kawaguchi, S. and Kuramitsu, S. (1998) J. Biol. Chem. 273, 18353-18364), enabled us to estimate the free energy required for the domain movement.
<StructureSection load='1c9c' size='340' side='right'caption='[[1c9c]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1c9c]] 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=1C9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9C FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PP3:ALANYL-PYRIDOXAL-5-PHOSPHATE'>PP3</scene></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=1c9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9c OCA], [https://pdbe.org/1c9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9c RCSB], [https://www.ebi.ac.uk/pdbsum/1c9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
== 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/c9/1c9c_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=1c9c ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1C9C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PP3 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C9C OCA].
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Free energy requirement for domain movement of an enzyme., Ishijima J, Nakai T, Kawaguchi S, Hirotsu K, Kuramitsu S, J Biol Chem. 2000 Jun 23;275(25):18939-45. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10858450 10858450]
[[Category: Aspartate transaminase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hirotsu, K.]]
[[Category: Hirotsu K]]
[[Category: Ishijima, J.]]
[[Category: Ishijima J]]
[[Category: Kawaguchi, S.]]
[[Category: Kawaguchi S]]
[[Category: Kuramitsu, S.]]
[[Category: Kuramitsu S]]
[[Category: Nakai, T.]]
[[Category: Nakai T]]
[[Category: PP3]]
[[Category: enzyme-substrate complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:16:43 2007''

Latest revision as of 09:41, 7 February 2024

ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATEASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE

Structural highlights

1c9c is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AAT_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1c9c, resolution 2.40Å

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