This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1khz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:25, 14 February 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1khz.gif|left|200px]]
 
-
{{Structure
+
==Structure of the ADPR-ase in complex with AMPCPR and Mg==
-
|PDB= 1khz |SIZE=350|CAPTION= <scene name='initialview01'>1khz</scene>, resolution 2.04&Aring;
+
<StructureSection load='1khz' size='340' side='right'caption='[[1khz]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=ADV:ALPHA-BETA+METHYLENE+ADP-RIBOSE'>ADV</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
+
<table><tr><td colspan='2'>[[1khz]] is a 2 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=1KHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KHZ FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/ADP-ribose_diphosphatase ADP-ribose diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.13 3.6.1.13] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04&#8491;</td></tr>
-
|GENE= ORF209 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADV:ALPHA-BETA+METHYLENE+ADP-RIBOSE'>ADV</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1khz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khz OCA], [https://pdbe.org/1khz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1khz RCSB], [https://www.ebi.ac.uk/pdbsum/1khz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1khz ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[1g0s|1G0S]], [[1g9q|1G9Q]], [[1ga7|1GA7]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1khz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khz OCA], [http://www.ebi.ac.uk/pdbsum/1khz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1khz RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/ADPP_ECOLI ADPP_ECOLI] Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process.<ref>PMID:11416161</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/kh/1khz_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=1khz ConSurf].
 +
<div style="clear:both"></div>
-
'''Structure of the ADPR-ase in complex with AMPCPR and Mg'''
+
==See Also==
-
 
+
*[[ADP-ribose pyrophosphatase|ADP-ribose pyrophosphatase]]
-
 
+
*[[ADP-ribose pyrophosphatase 3D structures|ADP-ribose pyrophosphatase 3D structures]]
-
==Overview==
+
== References ==
-
Escherichia coli ADP-ribose (ADPR) pyrophosphatase (ADPRase), a Nudix enzyme, catalyzes the Mg(2+)-dependent hydrolysis of ADP-ribose to AMP and ribose 5-phosphate. ADPR hydrolysis experiments conducted in the presence of H(2)(18)O and analyzed by electrospray mass spectrometry showed that the ADPRase-catalyzed reaction takes place through nucleophilic attack at the adenosyl phosphate. The structure of ADPRase in complex with Mg(2+) and a nonhydrolyzable ADPR analogue, alpha,beta-methylene ADP-ribose, reveals an active site water molecule poised for nucleophilic attack on the adenosyl phosphate. This water molecule is activated by two magnesium ions, and its oxygen contacts the target phosphorus (P-O distance of 3.0 A) and forms an angle of 177 degrees with the scissile bond, suggesting an associative mechanism. A third Mg(2+) ion bridges the two phosphates and could stabilize the negative charge of the leaving group, ribose 5-phosphate. The structure of the ternary complex also shows that loop L9 moves fully 10 A from its position in the free enzyme, forming a tighter turn and bringing Glu 162 to its catalytic position. These observations indicate that as part of the catalytic mechanism, the ADPRase cycles between an open (free enzyme) and a closed (substrate-metal complex) conformation. This cycling may be important in preventing nonspecific hydrolysis of other nucleotides.
+
<references/>
-
 
+
__TOC__
-
==About this Structure==
+
</StructureSection>
-
1KHZ 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=1KHZ OCA].
+
-
 
+
-
==Reference==
+
-
Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase., Gabelli SB, Bianchet MA, Ohnishi Y, Ichikawa Y, Bessman MJ, Amzel LM, Biochemistry. 2002 Jul 30;41(30):9279-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12135348 12135348]
+
-
[[Category: ADP-ribose diphosphatase]]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Amzel, L M.]]
+
[[Category: Amzel LM]]
-
[[Category: Bessman, M J.]]
+
[[Category: Bessman MJ]]
-
[[Category: Bianchet, M A.]]
+
[[Category: Bianchet MA]]
-
[[Category: Gabelli, S B.]]
+
[[Category: Gabelli SB]]
-
[[Category: adp-ribose pyrophosphatase]]
+
-
[[Category: ampcpr]]
+
-
[[Category: nudix]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:48:52 2008''
+

Current revision

Structure of the ADPR-ase in complex with AMPCPR and Mg

PDB ID 1khz

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1khz"
Personal tools