3d93

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:42, 30 August 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3d93.png|left|200px]]
 
-
<!--
+
==Apo Human carbonic anhydrase II bound with substrate carbon dioxide==
-
The line below this paragraph, containing "STRUCTURE_3d93", creates the "Structure Box" on the page.
+
<StructureSection load='3d93' size='340' side='right'caption='[[3d93]], [[Resolution|resolution]] 1.10&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'>[[3d93]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D93 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]] 1.1&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-
{{STRUCTURE_3d93| PDB=3d93 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d93 OCA], [https://pdbe.org/3d93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d93 RCSB], [https://www.ebi.ac.uk/pdbsum/3d93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d93 ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[https://omim.org/entry/259730 259730]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>
 +
== 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/d9/3d93_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=3d93 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The visualization at near atomic resolution of transient substrates in the active site of enzymes is fundamental to fully understanding their mechanism of action. Here we show the application of using CO(2)-pressurized, cryo-cooled crystals to capture the first step of CO(2) hydration catalyzed by the zinc-metalloenzyme human carbonic anhydrase II, the binding of substrate CO(2), for both the holo and the apo (without zinc) enzyme to 1.1A resolution. Until now, the feasibility of such a study was thought to be technically too challenging because of the low solubility of CO(2) and the fast turnover to bicarbonate by the enzyme (Liang, J. Y., and Lipscomb, W. N. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 3675-3679). These structures provide insight into the long hypothesized binding of CO(2) in a hydrophobic pocket at the active site and demonstrate that the zinc does not play a critical role in the binding or orientation of CO(2). This method may also have a much broader implication for the study of other enzymes for which CO(2) is a substrate or product and for the capturing of transient substrates and revealing hydrophobic pockets in proteins.
-
===Apo Human carbonic anhydrase II bound with substrate carbon dioxide===
+
Entrapment of carbon dioxide in the active site of carbonic anhydrase II.,Domsic JF, Avvaru BS, Kim CU, Gruner SM, Agbandje-McKenna M, Silverman DN, McKenna R J Biol Chem. 2008 Nov 7;283(45):30766-71. Epub 2008 Sep 2. PMID:18768466<ref>PMID:18768466</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3d93" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_18768466}}, adds the Publication Abstract to the page
+
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 18768466 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_18768466}}
+
__TOC__
-
 
+
</StructureSection>
-
==Disease==
+
-
Known disease associated with this structure: Hypercalciuria, absorptive, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605205 605205]]
+
-
 
+
-
==About this Structure==
+
-
3D93 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D93 OCA].
+
-
 
+
-
==Reference==
+
-
Entrapment of carbon dioxide in the active site of carbonic anhydrase II., Domsic JF, Avvaru BS, Kim CU, Gruner SM, Agbandje-McKenna M, Silverman DN, McKenna R, J Biol Chem. 2008 Nov 7;283(45):30766-71. Epub 2008 Sep 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18768466 18768466]
+
-
[[Category: Carbonate dehydratase]]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
+
[[Category: Avvaru BS]]
-
[[Category: Acetylation]]
+
[[Category: Domsic JF]]
-
[[Category: Cytoplasm]]
+
[[Category: McKenna R]]
-
[[Category: Disease mutation]]
+
-
[[Category: Lyase]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Polymorphism]]
+
-
[[Category: Substrate-bound]]
+
-
[[Category: Zinc]]
+
-
[[Category: Zinc metalloenzyme]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 24 20:28:40 2008''
+

Current revision

Apo Human carbonic anhydrase II bound with substrate carbon dioxide

PDB ID 3d93

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/3d93"
Personal tools