2jk0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2jk0" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:2jk0.png|left|200px]]
+
==STRUCTURAL AND FUNCTIONAL INSIGHTS INTO ERWINIA CAROTOVORA L-ASPARAGINASE==
 +
<StructureSection load='2jk0' size='340' side='right' caption='[[2jk0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
[[2jk0]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JK0 OCA]. <br>
 +
<b>Related:</b> [[2vm7|2vm7]]<br>
 +
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jk/2jk0_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
== Publication Abstract from PubMed ==
 +
Bacterial L-asparaginases are enzymes that catalyze the hydrolysis of l-asparagine to aspartic acid. For the past 30 years, these enzymes have been used as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia. Their intrinsic low-rate glutaminase activity, however, causes serious side-effects, including neurotoxicity, hepatitis, coagulopathy, and other dysfunctions. Erwinia carotovora asparaginase shows decreased glutaminase activity, so it is believed to have fewer side-effects in leukemia therapy. To gain detailed insights into the properties of E. carotovora asparaginase, combined crystallographic, thermal stability and cytotoxic experiments were performed. The crystal structure of E. carotovoral-asparaginase in the presence of L-Asp was determined at 2.5 A resolution and refined to an R cryst of 19.2 (R free = 26.6%) with good stereochemistry. Cytotoxicity measurements revealed that E. carotovora asparaginase is 30 times less toxic than the Escherichia coli enzyme against human leukemia cell lines. Moreover, denaturing experiments showed that E. carotovora asparaginase has decreased thermodynamic stability as compared to the E. coli enzyme and is rapidly inactivated in the presence of urea. On the basis of these results, we propose that E. carotovora asparaginase has limited potential as an antileukemic drug, despite its promising low glutaminase activity. Our analysis may be applicable to the therapeutic evaluation of other asparaginases as well.
-
<!--
+
Structural and functional insights into Erwinia carotovora L-asparaginase.,Papageorgiou AC, Posypanova GA, Andersson CS, Sokolov NN, Krasotkina J FEBS J. 2008 Sep;275(17):4306-16. Epub 2008 Jul 21. PMID:18647344<ref>PMID:18647344</ref>
-
The line below this paragraph, containing "STRUCTURE_2jk0", 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_2jk0| PDB=2jk0 | SCENE= }}
+
-
===STRUCTURAL AND FUNCTIONAL INSIGHTS INTO ERWINIA CAROTOVORA L-ASPARAGINASE===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
== References ==
-
 
+
<references/>
-
<!--
+
__TOC__
-
The line below this paragraph, {{ABSTRACT_PUBMED_18647344}}, adds the Publication Abstract to the page
+
</StructureSection>
-
(as it appears on PubMed at http://www.pubmed.gov), where 18647344 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_18647344}}
+
-
 
+
-
==About this Structure==
+
-
[[2jk0]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JK0 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:018647344</ref><references group="xtra"/>
+
[[Category: Asparaginase]]
[[Category: Asparaginase]]
[[Category: Pectobacterium carotovorum]]
[[Category: Pectobacterium carotovorum]]

Revision as of 08:23, 30 April 2014

STRUCTURAL AND FUNCTIONAL INSIGHTS INTO ERWINIA CAROTOVORA L-ASPARAGINASE

2jk0, resolution 2.50Å

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/2jk0"
Personal tools