1cq6: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1cq6.jpg|left|200px]]


{{Structure
==ASPARTATE AMINOTRANSFERASE COMPLEX WITH C4-PYRIDOXAL-5P-PHOSPHATE==
|PDB= 1cq6 |SIZE=350|CAPTION= <scene name='initialview01'>1cq6</scene>, resolution 2.7&Aring;
<StructureSection load='1cq6' size='340' side='right'caption='[[1cq6]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PY4:2-[O-PHOSPHONOPYRIDOXYL]-AMINO- BUTYRIC ACID'>PY4</scene>
<table><tr><td colspan='2'>[[1cq6]] 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=1CQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQ6 FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PY4:2-[O-PHOSPHONOPYRIDOXYL]-AMINO-+BUTYRIC+ACID'>PY4</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=1cq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cq6 OCA], [https://pdbe.org/1cq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cq6 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/cq/1cq6_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=1cq6 ConSurf].
<div style="clear:both"></div>


'''ASPARTATE AMINOTRANSFERASE COMPLEX WITH C4-PYRIDOXAL-5P-PHOSPHATE'''
==See Also==
 
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1CQ6 is a [[Single protein]] structure of sequence 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=1CQ6 OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/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: PY4]]
[[Category: enzyme-substrate complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:27:32 2008''

Latest revision as of 06:44, 7 February 2024

ASPARTATE AMINOTRANSFERASE COMPLEX WITH C4-PYRIDOXAL-5P-PHOSPHATE

1cq6, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1cq6&oldid=4041240"