1zpe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:12, 23 August 2023) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1zpe.gif|left|200px]]<br /><applet load="1zpe" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1zpe, resolution 1.70&Aring;" />
 
-
'''Arginase I covalently modified with butylamine at Q19C'''<br />
 
-
==Overview==
+
==Arginase I covalently modified with butylamine at Q19C==
 +
<StructureSection load='1zpe' size='340' side='right'caption='[[1zpe]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1zpe]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZPE 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]] 1.7&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BBC:3-[(4-AMINOBUTYL)SULFINYL]-2-IMINOPROPAN-1-OL'>BBC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1zpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zpe OCA], [https://pdbe.org/1zpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zpe RCSB], [https://www.ebi.ac.uk/pdbsum/1zpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zpe ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ARGI1_RAT ARGI1_RAT]
 +
== 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/zp/1zpe_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=1zpe ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
Rat liver arginase (arginase I) is potently inactivated by diethyl pyrocarbonate, with a second-order rate constant of 113M(-1)s(-1) for the inactivation process at pH 7.0, 25 degrees C. Partial protection from inactivation is provided by the product of the reaction, l-ornithine, while nearly complete protection is afforded by the inhibitor pair, l-ornithine and borate. The role of H141 has been probed by mutagenesis, chemical modulation, and X-ray diffraction. The hyper-reactivity of H141 towards diethyl pyrocarbonate can be explained by its proximity to E277. A proton shuttling role for H141 is supported by its conformational mobility observed among the known arginase structures. H141 is proposed to serve as an acid/base catalyst, deprotonating the metal-bridging water molecule to generate the metal-bridging hydroxide nucleophile, and by protonating the amino group of the product to facilitate its departure.
Rat liver arginase (arginase I) is potently inactivated by diethyl pyrocarbonate, with a second-order rate constant of 113M(-1)s(-1) for the inactivation process at pH 7.0, 25 degrees C. Partial protection from inactivation is provided by the product of the reaction, l-ornithine, while nearly complete protection is afforded by the inhibitor pair, l-ornithine and borate. The role of H141 has been probed by mutagenesis, chemical modulation, and X-ray diffraction. The hyper-reactivity of H141 towards diethyl pyrocarbonate can be explained by its proximity to E277. A proton shuttling role for H141 is supported by its conformational mobility observed among the known arginase structures. H141 is proposed to serve as an acid/base catalyst, deprotonating the metal-bridging water molecule to generate the metal-bridging hydroxide nucleophile, and by protonating the amino group of the product to facilitate its departure.
-
==About this Structure==
+
Probing the role of the hyper-reactive histidine residue of arginase.,Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE Arch Biochem Biophys. 2005 Dec 1;444(1):15-26. Epub 2005 Oct 13. PMID:16266687<ref>PMID:16266687</ref>
-
1ZPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPE OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Probing the role of the hyper-reactive histidine residue of arginase., Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE, Arch Biochem Biophys. 2005 Dec 1;444(1):15-26. Epub 2005 Oct 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16266687 16266687]
+
</div>
-
[[Category: Arginase]]
+
<div class="pdbe-citations 1zpe" style="background-color:#fffaf0;"></div>
-
[[Category: Rattus norvegicus]]
+
-
[[Category: Single protein]]
+
-
[[Category: Ash, D E.]]
+
-
[[Category: Cama, E.]]
+
-
[[Category: Christianson, D W.]]
+
-
[[Category: Colleluori, D M.]]
+
-
[[Category: Compher, K.]]
+
-
[[Category: Cox, J D.]]
+
-
[[Category: Emig, F A.]]
+
-
[[Category: Han, S.]]
+
-
[[Category: Jude, K.]]
+
-
[[Category: Reczkowski, R S.]]
+
-
[[Category: Scolnick, L R.]]
+
-
[[Category: Viola, R E.]]
+
-
[[Category: MN]]
+
-
[[Category: chemically modified enzyme]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:49 2008''
+
==See Also==
 +
*[[Arginase 3D structures|Arginase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Rattus norvegicus]]
 +
[[Category: Ash DE]]
 +
[[Category: Cama E]]
 +
[[Category: Christianson DW]]
 +
[[Category: Colleluori DM]]
 +
[[Category: Compher K]]
 +
[[Category: Cox JD]]
 +
[[Category: Emig FA]]
 +
[[Category: Han S]]
 +
[[Category: Jude K]]
 +
[[Category: Reczkowski RS]]
 +
[[Category: Scolnick LR]]
 +
[[Category: Viola RE]]

Current revision

Arginase I covalently modified with butylamine at Q19C

PDB ID 1zpe

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/1zpe"
Personal tools