1i6p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:22, 9 August 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1i6p.jpg|left|200px]]
 
-
<!--
+
==CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)==
-
The line below this paragraph, containing "STRUCTURE_1i6p", creates the "Structure Box" on the page.
+
<StructureSection load='1i6p' size='340' side='right'caption='[[1i6p]], [[Resolution|resolution]] 2.00&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'>[[1i6p]] 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=1I6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6P 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&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
{{STRUCTURE_1i6p| PDB=1i6p | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6p OCA], [https://pdbe.org/1i6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i6p RCSB], [https://www.ebi.ac.uk/pdbsum/1i6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6p ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CAN_ECOLI CAN_ECOLI]
 +
== 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/i6/1i6p_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=1i6p ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Carbonic anhydrases fall into three distinct evolutionary and structural classes: alpha, beta, and gamma. The beta-class carbonic anhydrases (beta-CAs) are widely distributed among higher plants, simple eukaryotes, eubacteria, and archaea. We have determined the crystal structure of ECCA, a beta-CA from Escherichia coli, to a resolution of 2.0 A. In agreement with the structure of the beta-CA from the chloroplast of the red alga Porphyridium purpureum, the active-site zinc in ECCA is tetrahedrally coordinated by the side chains of four conserved residues. These results confirm the observation of a unique pattern of zinc ligation in at least some beta-CAS: The absence of a water molecule in the inner coordination sphere is inconsistent with known mechanisms of CA activity. ECCA activity is highly pH-dependent in the physiological range, and its expression in yeast complements an oxygen-sensitive phenotype displayed by a beta-CA-deletion strain. The structural and biochemical characterizations of ECCA presented here and the comparisons with other beta-CA structures suggest that ECCA can adopt two distinct conformations displaying widely divergent catalytic rates.
-
'''CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)'''
+
Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.,Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY Protein Sci. 2001 May;10(5):911-22. PMID:11316870<ref>PMID:11316870</ref>
-
 
+
-
 
+
-
==Overview==
+
-
Carbonic anhydrases fall into three distinct evolutionary and structural classes: alpha, beta, and gamma. The beta-class carbonic anhydrases (beta-CAs) are widely distributed among higher plants, simple eukaryotes, eubacteria, and archaea. We have determined the crystal structure of ECCA, a beta-CA from Escherichia coli, to a resolution of 2.0 A. In agreement with the structure of the beta-CA from the chloroplast of the red alga Porphyridium purpureum, the active-site zinc in ECCA is tetrahedrally coordinated by the side chains of four conserved residues. These results confirm the observation of a unique pattern of zinc ligation in at least some beta-CAS: The absence of a water molecule in the inner coordination sphere is inconsistent with known mechanisms of CA activity. ECCA activity is highly pH-dependent in the physiological range, and its expression in yeast complements an oxygen-sensitive phenotype displayed by a beta-CA-deletion strain. The structural and biochemical characterizations of ECCA presented here and the comparisons with other beta-CA structures suggest that ECCA can adopt two distinct conformations displaying widely divergent catalytic rates.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
1I6P 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=1I6P OCA].
+
</div>
 +
<div class="pdbe-citations 1i6p" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity., Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY, Protein Sci. 2001 May;10(5):911-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11316870 11316870]
+
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
-
[[Category: Carbonate dehydratase]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Cronk, J D.]]
+
[[Category: Cronk JD]]
-
[[Category: Cronk, M R.]]
+
[[Category: Cronk MR]]
-
[[Category: Endrizzi, J A.]]
+
[[Category: Endrizzi JA]]
-
[[Category: Neill, J W.O.]]
+
[[Category: O'Neill JW]]
-
[[Category: Zhang, K Y.J.]]
+
[[Category: Zhang KYJ]]
-
[[Category: Carbonic anhydrase]]
+
-
[[Category: Crystal structure]]
+
-
[[Category: Mad phasing]]
+
-
[[Category: Metalloenzyme]]
+
-
[[Category: Ph-dependent activity]]
+
-
[[Category: Zinc coordination]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:38:19 2008''
+

Current revision

CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)

PDB ID 1i6p

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/1i6p"
Personal tools