2e4g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:34, 25 October 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2e4g.gif|left|200px]]
 
-
<!--
+
==RebH with bound L-Trp==
-
The line below this paragraph, containing "STRUCTURE_2e4g", creates the "Structure Box" on the page.
+
<StructureSection load='2e4g' size='340' side='right'caption='[[2e4g]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2e4g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentzea_aerocolonigenes Lentzea aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E4G FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
-
{{STRUCTURE_2e4g| PDB=2e4g | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4g OCA], [https://pdbe.org/2e4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e4g RCSB], [https://www.ebi.ac.uk/pdbsum/2e4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e4g ProSAT]</span></td></tr>
-
 
+
</table>
-
'''RebH with bound L-Trp'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/REBH_LENAE REBH_LENAE] Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the chlorination of tryptophan (Trp) at C7 position to yield 7-chlorotryptophan. The reaction between FADH2, Cl-, and O2 generates the powerful oxidant HOCl, which is presumed to carry out the chlorination reaction. The reaction of HOCl with the active site Lys-79 generates a lysine chloramine, which plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes. It is also able to use bromide ions to generate monobrominated Trp.<ref>PMID:11983340</ref> <ref>PMID:15743914</ref> <ref>PMID:17260957</ref>
-
 
+
== Evolutionary Conservation ==
-
==Overview==
+
[[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/e4/2e4g_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=2e4g ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
The flavin-dependent halogenase RebH catalyzes the formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin. The reaction of FADH2, Cl-, and O2 in the active site generates the powerful oxidant HOCl, which was presumed to carry out the chlorination reaction. Herein, we demonstrate the formation of a long-lived chlorinating intermediate (t1/2 = 63 h at 4 degrees C) when RebH, FADH2, Cl-, and O2 react in the absence of substrate tryptophan. This intermediate remained on the enzyme after removal of FAD and transferred chlorine to tryptophan with kinetically competent rates. The identity of this intermediate is suggested by the X-ray crystal structure of RebH, which revealed an active site Lys79 located in a central position between flavin and tryptophan binding sites and just 4.1 A above C7 of tryptophan. The chlorinating species is proposed to be a Lys-epsilonNH-Cl (lysine chloramine) from reaction of enzyme-generated HOCl with the active site Lys79. This covalent enzyme chloramine likely plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes.
The flavin-dependent halogenase RebH catalyzes the formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin. The reaction of FADH2, Cl-, and O2 in the active site generates the powerful oxidant HOCl, which was presumed to carry out the chlorination reaction. Herein, we demonstrate the formation of a long-lived chlorinating intermediate (t1/2 = 63 h at 4 degrees C) when RebH, FADH2, Cl-, and O2 react in the absence of substrate tryptophan. This intermediate remained on the enzyme after removal of FAD and transferred chlorine to tryptophan with kinetically competent rates. The identity of this intermediate is suggested by the X-ray crystal structure of RebH, which revealed an active site Lys79 located in a central position between flavin and tryptophan binding sites and just 4.1 A above C7 of tryptophan. The chlorinating species is proposed to be a Lys-epsilonNH-Cl (lysine chloramine) from reaction of enzyme-generated HOCl with the active site Lys79. This covalent enzyme chloramine likely plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes.
-
==About this Structure==
+
Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases.,Yeh E, Blasiak LC, Koglin A, Drennan CL, Walsh CT Biochemistry. 2007 Feb 6;46(5):1284-92. PMID:17260957<ref>PMID:17260957</ref>
-
2E4G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lechevalieria_aerocolonigenes Lechevalieria aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4G OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases., Yeh E, Blasiak LC, Koglin A, Drennan CL, Walsh CT, Biochemistry. 2007 Feb 6;46(5):1284-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17260957 17260957]
+
</div>
-
[[Category: Lechevalieria aerocolonigenes]]
+
<div class="pdbe-citations 2e4g" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
== References ==
-
[[Category: Blasiak, L C.]]
+
<references/>
-
[[Category: Drennan, C L.]]
+
__TOC__
-
[[Category: Flavin-binding]]
+
</StructureSection>
-
[[Category: Rebeccamycin biosynthesis]]
+
[[Category: Large Structures]]
-
[[Category: Tryptophan-7-halogenase]]
+
[[Category: Lentzea aerocolonigenes]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:54:08 2008''
+
[[Category: Blasiak LC]]
 +
[[Category: Drennan CL]]

Current revision

RebH with bound L-Trp

PDB ID 2e4g

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/2e4g"
Personal tools