1add: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1add" size="450" color="white" frame="true" align="right" spinBox="true" caption="1add, resolution 2.4Å" /> '''A PRE-TRANSITION STAT...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1add.gif|left|200px]]<br /><applet load="1add" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1add, resolution 2.4&Aring;" />
'''A PRE-TRANSITION STATE MIMIC OF AN ENZYME: X-RAY STRUCTURE OF ADENOSINE DEAMINASE WITH BOUND 1-DEAZA-ADENOSINE AND ZINC-ACTIVATED WATER'''<br />


==Overview==
==A PRE-TRANSITION STATE MIMIC OF AN ENZYME: X-RAY STRUCTURE OF ADENOSINE DEAMINASE WITH BOUND 1-DEAZA-ADENOSINE AND ZINC-ACTIVATED WATER==
The refined 2.4-A structure of adenosine deaminase, recently discovered to, be a zinc metalloenzyme [Wilson, D. K., Rudolph, F. B., &amp; Quiocho, F. A., (1991) Science 252, 1278-1284], complexed with the ground-state analog, 1-deazaadenosine shows the mode of binding of the analog and, unexpectedly, a zinc-activated water (hydroxide). This structure of a, pre-transition-state mimic, combined with that previously determined for, the complex with 6(R)-hydroxy-1,6-dihydropurine ribonucleoside, a nearly, ideal transition-state analog, sheds new understanding of the precise, stereospecificity and hydrolytic catalysis of an important and, well-characterized member of a large group of zinc metalloenzymes. As both, of these excellent mimics were generated in the active site, they, demonstrate a powerful means of dissecting the course of an enzymatic, reaction by direct crystallographic analysis.
<StructureSection load='1add' size='340' side='right'caption='[[1add]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1add]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADD 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=1DA:1-DEAZA-ADENOSINE'>1DA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1add OCA], [https://pdbe.org/1add PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1add RCSB], [https://www.ebi.ac.uk/pdbsum/1add PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1add ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ADA_MOUSE ADA_MOUSE] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).
== 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/ad/1add_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=1add ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1ADD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and 1DA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ADD OCA].
*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water., Wilson DK, Quiocho FA, Biochemistry. 1993 Feb 23;32(7):1689-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8439534 8439534]
[[Category: Large Structures]]
[[Category: Adenosine deaminase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Quiocho FA]]
[[Category: Quiocho, F.A.]]
[[Category: Wilson DK]]
[[Category: Wilson, D.K.]]
[[Category: 1DA]]
[[Category: ZN]]
[[Category: hydrolase(acting in cyclicamidines)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:46:15 2007''

Latest revision as of 09:29, 7 February 2024

A PRE-TRANSITION STATE MIMIC OF AN ENZYME: X-RAY STRUCTURE OF ADENOSINE DEAMINASE WITH BOUND 1-DEAZA-ADENOSINE AND ZINC-ACTIVATED WATERA PRE-TRANSITION STATE MIMIC OF AN ENZYME: X-RAY STRUCTURE OF ADENOSINE DEAMINASE WITH BOUND 1-DEAZA-ADENOSINE AND ZINC-ACTIVATED WATER

Structural highlights

1add is a 1 chain structure with sequence from Mus musculus. 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

ADA_MOUSE Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).

Evolutionary Conservation

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

See Also

1add, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1add&oldid=4040048"