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.


1g15

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1g15" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g15, resolution 1.9&Aring;" /> '''CO-CRYSTAL OF E. COLI...)
Current revision (07:21, 7 February 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1g15.jpg|left|200px]]<br /><applet load="1g15" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1g15, resolution 1.9&Aring;" />
 
-
'''CO-CRYSTAL OF E. COLI RNASE HI WITH TWO MN2+ IONS BOUND IN THE THE ACTIVE SITE'''<br />
 
-
==Overview==
+
==CO-CRYSTAL OF E. COLI RNASE HI WITH TWO MN2+ IONS BOUND IN THE THE ACTIVE SITE==
-
Ribonuclease H (RNase H) selectively degrades the RNA strand of RNA.DNA, hybrids in a divalent cation-dependent manner. Previous structural studies, revealed a single Mg(2+) ion-binding site in Escherichia coli RNase HI. In, the crystal structure of the related RNase H domain of human, immunodeficiency virus reverse transcriptase, however, two Mn(2+) ions, were observed suggesting a different mode of metal binding. E. coli RNase, HI shows catalytic activity in the presence of Mg(2+) or Mn(2+) ions, but, these two metals show strikingly different optimal concentrations. Mg(2+), ions are required in millimolar concentrations, but Mn(2+) ions are only, required in micromolar quantities. Based upon the metal dependence of E., coli RNase HI activity, we proposed an activation/attenuation model in, which one metal is required for catalysis, and binding of a second metal, is inhibitory. We have now solved the co-crystal structure of E. coli, RNase HI with Mn(2+) ions at 1.9-A resolution. Two octahedrally, coordinated Mn(2+) ions are seen to bind to the enzyme-active site., Residues Asp-10, Glu-48, and Asp-70 make direct (inner sphere), coordination contacts to the first (activating) metal, whereas residues, Asp-10 and Asp-134 make direct contacts to the second (attenuating) metal., This structure is consistent with biochemical evidence suggesting that two, metal ions may bind RNase H but liganding a second ion inhibits RNase H, activity.
+
<StructureSection load='1g15' size='340' side='right'caption='[[1g15]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1g15]] is a 1 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=1G15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G15 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]] 1.9&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1g15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g15 OCA], [https://pdbe.org/1g15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g15 RCSB], [https://www.ebi.ac.uk/pdbsum/1g15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g15 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/RNH_ECOLI RNH_ECOLI] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. RNase H participates in DNA replication; it helps to specify the origin of genomic replication by suppressing initiation at origins other than the oriC locus; along with the 5'-3' exonuclease of pol1, it removes RNA primers from the Okazaki fragments of lagging strand synthesis; and it defines the origin of replication for ColE1-type plasmids by specific cleavage of an RNA preprimer.[HAMAP-Rule:MF_00042]
 +
== 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/g1/1g15_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=1g15 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1G15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G15 OCA].
+
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site., Goedken ER, Marqusee S, J Biol Chem. 2001 Mar 9;276(10):7266-71. Epub 2000 Nov 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11083878 11083878]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Ribonuclease H]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Goedken ER]]
-
[[Category: Goedken, E.R.]]
+
[[Category: Marqusee S]]
-
[[Category: Marqusee, S.]]
+
-
[[Category: MN]]
+
-
[[Category: activation/attenuation mechanism]]
+
-
[[Category: divalent metal binding]]
+
-
[[Category: nuclease]]
+
-
[[Category: ribonuclease h]]
+
-
[[Category: rnase h]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:36:44 2007''
+

Current revision

CO-CRYSTAL OF E. COLI RNASE HI WITH TWO MN2+ IONS BOUND IN THE THE ACTIVE SITE

PDB ID 1g15

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/1g15"
Personal tools