1poh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1poh" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:1poh.png|left|200px]]
+
==THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION==
 +
<StructureSection load='1poh' size='340' side='right' caption='[[1poh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1poh]] is a 1 chain structure with 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=1POH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1POH FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1poh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1poh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1poh RCSB], [http://www.ebi.ac.uk/pdbsum/1poh PDBsum]</span></td></tr>
 +
<table>
 +
== 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/po/1poh_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>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The x-ray structure of Escherichia coli HPr has been redetermined at 2.0-A resolution. In contrast to the previous study (El-Kabbani, O. A. L., Waygood, E. B., and Delbaere, L. T. J. (1987) J. Biol. Chem. 262, 12926-12929), the overall structure is, in general, similar to other reported NMR and x-ray HPr structures, although there are some important differences in detail. The overall folding topology of HPr is a classical open-faced beta-sandwich, consisting of four antiparallel beta-strands and three alpha-helices. The least square refinement produced an R index of 0.135 for all measured unique data between 8.0 and 2.0 A resolution. The active center consists of His15 which is hydrogen bonded to a sulfate anion, and Arg17 which has a fully open conformation. This corresponds to the first observed "semi-closed" conformation of the active center of HPr. The Streptococcus faecalis HPr structure (Jia, Z., Vandonselaar, M., Quail, J. W., and Delbaere, L. T. J. (1993) Nature 361, 94-97) has the "open" conformation in which the side chains of His15 and Arg17 are directed as far away from each other as possible. The Bacillus subtilis HPr (Herzberg, O., Reddy, P., Sutrina, S., Saier, M. H., Jr., Reizer, J., and Kapadia, G. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2499-2503) has the "closed" conformation in which the side chains of His15 and Arg17 are close together with a sulfate anion located in the active center. The open conformation represents the unphosphorylated form of HPr whereas the closed conformation likely resembles the phosphorylated form of HPr. The semi-closed conformation observed in the E. coli HPr structure could represent a structural intermediate on the phosphorylation/dephosphorylation pathway of HPr.
-
{{STRUCTURE_1poh| PDB=1poh | SCENE= }}
+
The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination.,Jia Z, Quail JW, Waygood EB, Delbaere LT J Biol Chem. 1993 Oct 25;268(30):22490-501. PMID:8226757<ref>PMID:8226757</ref>
-
===THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
-
{{ABSTRACT_PUBMED_8226757}}
+
==See Also==
-
 
+
*[[Phosphocarrier protein HPr|Phosphocarrier protein HPr]]
-
==About this Structure==
+
== References ==
-
[[1poh]] is a 1 chain structure with 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=1POH OCA].
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
<ref group="xtra">PMID:008226757</ref><ref group="xtra">PMID:016477599</ref><ref group="xtra">PMID:016488431</ref><references group="xtra"/>
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Delbaere, L.]]
[[Category: Delbaere, L.]]

Revision as of 19:40, 28 September 2014

THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION

1poh, resolution 2.00Å

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/1poh"
Views
Personal tools
Navigation
Toolbox