3l6w

From Proteopedia

(Difference between revisions)

Current revision

Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin

Structural highlights

3l6w is a 2 chain structure with sequence from Megathura crenulata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 4Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HCY1_MEGCR Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Haemocyanins are multimeric oxygen transport proteins, which bind oxygen to type 3 copper sites. Arthropod haemocyanins contain 75-kDa subunits, whereas molluscan haemocyanins contain 350-400-kDa subunits comprising seven or eight different 50 kDa FUs (functional units) designated FU-a to FU-h, each with an active site. FU-h possesses a tail of 100 amino acids not present in the other FUs. In the present study we show by X-ray crystallography that in FU-h of KLH1 (keyhole-limpet-haemocyanin isoform 1) the structure of the tail domain is cupredoxin-like but contains no copper. The copper-free domain 3 in arthropod haemocyanin subunits has also recently been reinterpreted as being cupredoxin-like. We propose that the cupredoxin-like domain in both haemocyanin types once served to upload copper to the active site of the oxygen-binding domain.

Cupredoxin-like domains in haemocyanins.,Jaenicke E, Buchler K, Markl J, Decker H, Barends TR Biochem J. 2010 Feb 24;426(3):373-8. PMID:20025608^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Swerdlow RD, Ebert RF, Lee P, Bonaventura C, Miller KI. Keyhole limpet hemocyanin: structural and functional characterization of two different subunits and multimers. Comp Biochem Physiol B Biochem Mol Biol. 1996 Mar;113(3):537-48. PMID:8829804 doi:10.1016/0305-0491(95)02091-8
↑ Jaenicke E, Buchler K, Markl J, Decker H, Barends TR. Cupredoxin-like domains in haemocyanins. Biochem J. 2010 Feb 24;426(3):373-8. PMID:20025608 doi:10.1042/BJ20091501

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3l6w"

@@ Line 1: / Line 1: @@
 ==Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin==
-<StructureSection load='3l6w' size='340' side='right' caption='[[3l6w]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
+<StructureSection load='3l6w' size='340' side='right'caption='[[3l6w]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3l6w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Megathura_crenulata Megathura crenulata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L6W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3l6w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Megathura_crenulata Megathura crenulata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L6W FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eu2|3eu2]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3l6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6w OCA], [http://pdbe.org/3l6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l6w RCSB], [http://www.ebi.ac.uk/pdbsum/3l6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l6w ProSAT]</span></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=3l6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6w OCA], [https://pdbe.org/3l6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l6w RCSB], [https://www.ebi.ac.uk/pdbsum/3l6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l6w ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/HCY1_MEGCR HCY1_MEGCR] Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.<ref>PMID:8829804</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/l6/3l6w_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/3l6w_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 32: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Megathura crenulata]]
-[[Category: Barends, T R.M]]
+[[Category: Barends TRM]]
-[[Category: Buechler, K]]
+[[Category: Buechler K]]
-[[Category: Decker, H]]
+[[Category: Decker H]]
-[[Category: Jaenicke, E]]
+[[Category: Jaenicke E]]
-[[Category: Markl, J]]
+[[Category: Markl J]]
-[[Category: Copper-binding protein]]
-[[Category: Cupredoxin domain]]
-[[Category: Hemocyanin]]
-[[Category: Metal-binding]]
-[[Category: Oxygen binding]]

3l6w

From Proteopedia

Current revision

Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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