1t4d: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1t4d.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1t4d", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1t4d|  PDB=1t4d  |  SCENE=  }}
'''Crystal structure of Escherichia coli aspartate beta-semialdehyde dehydrogenase (EcASADH), at 1.95 Angstrom resolution'''


==Crystal structure of Escherichia coli aspartate beta-semialdehyde dehydrogenase (EcASADH), at 1.95 Angstrom resolution==
<StructureSection load='1t4d' size='340' side='right'caption='[[1t4d]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1t4d]] 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=1T4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T4D 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]] 1.95&#8491;</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=1t4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4d OCA], [https://pdbe.org/1t4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t4d RCSB], [https://www.ebi.ac.uk/pdbsum/1t4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t4d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DHAS_ECOLI DHAS_ECOLI] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.<ref>PMID:6102909</ref> <ref>PMID:11368768</ref>
== 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/t4/1t4d_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=1t4d ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two high-resolution structures have been determined for Eschericia coli aspartate beta-semialdehyde dehydrogenase (ecASADH), an enzyme of the aspartate biosynthetic pathway, which is a potential target for novel antimicrobial drugs. Both ASADH structures were of the open form and were refined to 1.95 A and 1.6 A resolution, allowing a more detailed comparison with the closed form of the enzyme than previously possible. A more complex scheme for domain closure is apparent with the subunit being split into two further sub-domains with relative motions about three hinge axes. Analysis of hinge data and torsion-angle difference plots is combined to allow the proposal of a detailed structural mechanism for ecASADH domain closure. Additionally, asymmetric distortions of individual subunits are identified, which form the basis for the previously reported "half-of-the-sites reactivity" (HOSR). A putative explanation of this arrangement is also presented, suggesting the HOSR system may provide a means for ecASADH to offset the energy required to remobilise flexible loops at the end of the reaction cycle, and hence avoid falling into an energy minimum.


==Overview==
High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase.,Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK J Mol Biol. 2004 Aug 13;341(3):797-806. PMID:15288787<ref>PMID:15288787</ref>
Two high-resolution structures have been determined for Eschericia coli aspartate beta-semialdehyde dehydrogenase (ecASADH), an enzyme of the aspartate biosynthetic pathway, which is a potential target for novel antimicrobial drugs. Both ASADH structures were of the open form and were refined to 1.95 A and 1.6 A resolution, allowing a more detailed comparison with the closed form of the enzyme than previously possible. A more complex scheme for domain closure is apparent with the subunit being split into two further sub-domains with relative motions about three hinge axes. Analysis of hinge data and torsion-angle difference plots is combined to allow the proposal of a detailed structural mechanism for ecASADH domain closure. Additionally, asymmetric distortions of individual subunits are identified, which form the basis for the previously reported "half-of-the-sites reactivity" (HOSR). A putative explanation of this arrangement is also presented, suggesting the HOSR system may provide a means for ecASADH to offset the energy required to remobilise flexible loops at the end of the reaction cycle, and hence avoid falling into an energy minimum.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1T4D 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=1T4D OCA].
</div>
<div class="pdbe-citations 1t4d" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase., Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK, J Mol Biol. 2004 Aug 13;341(3):797-806. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15288787 15288787]
*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
[[Category: Aspartate-semialdehyde dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dhaliwal, B.]]
[[Category: Dhaliwal B]]
[[Category: Hawkins, A R.]]
[[Category: Hawkins AR]]
[[Category: Lockyer, M.]]
[[Category: Lockyer M]]
[[Category: Nichols, C E.]]
[[Category: Nichols CE]]
[[Category: Stammers, D K.]]
[[Category: Stammers DK]]
[[Category: Asadh]]
[[Category: Aspartate semialdehyde dehydrogenase]]
[[Category: Domain movement]]
[[Category: Hosr]]
[[Category: Lysine biosynthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:30:43 2008''

Latest revision as of 06:25, 23 August 2023

Crystal structure of Escherichia coli aspartate beta-semialdehyde dehydrogenase (EcASADH), at 1.95 Angstrom resolution

1t4d, resolution 1.95Å

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=1t4d&oldid=3839581"