1f21

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:09, 7 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1f21.jpg|left|200px]]
 
-
<!--
+
==DIVALENT METAL COFACTOR BINDING IN THE KINETIC FOLDING TRAJECTORY OF E. COLI RIBONUCLEASE HI==
-
The line below this paragraph, containing "STRUCTURE_1f21", creates the "Structure Box" on the page.
+
<StructureSection load='1f21' size='340' side='right'caption='[[1f21]], [[Resolution|resolution]] 1.40&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'>[[1f21]] 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=1F21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F21 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]] 1.4&#8491;</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=1f21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f21 OCA], [https://pdbe.org/1f21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f21 RCSB], [https://www.ebi.ac.uk/pdbsum/1f21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f21 ProSAT]</span></td></tr>
-
{{STRUCTURE_1f21| PDB=1f21 | SCENE= }}
+
</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/f2/1f21_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=1f21 ConSurf].
 +
<div style="clear:both"></div>
-
'''DIVALENT METAL COFACTOR BINDING IN THE KINETIC FOLDING TRAJECTORY OF E. COLI RIBONUCLEASE HI'''
+
==See Also==
-
 
+
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
Proteins often require cofactors to perform their biological functions and must fold in the presence of their cognate ligands. Using circular dichroism spectroscopy. we investigated the effects of divalent metal binding upon the folding pathway of Escherichia coli RNase HI. This enzyme binds divalent metal in its active site, which is proximal to the folding core of RNase HI as defined by hydrogen/deuterium exchange studies. Metal binding increases the apparent stability of native RNase HI chiefly by reducing the unfolding rate. As with the apo-form of the protein, refolding from high denaturant concentrations in the presence of Mg2+ follows three-state kinetics: formation of a rapid burst phase followed by measurable single exponential kinetics. Therefore, the overall folding pathway of RNase HI is minimally perturbed by the presence of metal ions. Our results indicate that the metal cofactor enters the active site pocket only after the enzyme reaches its native fold, and therefore, divalent metal binding stabilizes the protein by decreasing its unfolding rate. Furthermore, the binding of the cofactor is dependent upon a carboxylate critical for activity (Asp10). A mutation in this residue (D10A) alters the folding kinetics in the absence of metal ions such that they are similar to those observed for the unaltered enzyme in the presence of metal.
+
-
 
+
-
==About this Structure==
+
-
1F21 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=1F21 OCA].
+
-
 
+
-
==Reference==
+
-
Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI., Goedken ER, Keck JL, Berger JM, Marqusee S, Protein Sci. 2000 Oct;9(10):1914-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106164 11106164]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Ribonuclease H]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Berger JM]]
-
[[Category: Berger, J M.]]
+
[[Category: Goedken ER]]
-
[[Category: Goedken, E R.]]
+
[[Category: Keck JL]]
-
[[Category: Keck, J L.]]
+
[[Category: Marqusee S]]
-
[[Category: Marqusee, S.]]
+
-
[[Category: Metal-binding protein]]
+
-
[[Category: Nuclease]]
+
-
[[Category: Protein folding]]
+
-
[[Category: Ribnuclease h]]
+
-
[[Category: Rnase h]]
+
-
[[Category: Rnase h*]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:47:34 2008''
+

Current revision

DIVALENT METAL COFACTOR BINDING IN THE KINETIC FOLDING TRAJECTORY OF E. COLI RIBONUCLEASE HI

PDB ID 1f21

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/1f21"
Personal tools